Phosphorus in PDB 1a81: Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam

Enzymatic activity of Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam

All present enzymatic activity of Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam:
2.7.1.112;

Protein crystallography data

The structure of Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam, PDB code: 1a81 was solved by K.Fuetterer, G.Waksman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 3.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 85.500, 146.900, 91.500, 90.00, 97.60, 90.00
R / Rfree (%) 22.6 / 31.7

Phosphorus Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Phosphorus atom in the Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam (pdb code 1a81). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 12 binding sites of Phosphorus where determined in the Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam, PDB code: 1a81:
Jump to Phosphorus binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Phosphorus binding site 1 out of 12 in 1a81

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Phosphorus binding site 1 out of 12 in the Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam within 5.0Å range:
probe atom residue distance (Å) B Occ
B:P170

b:36.7
occ:1.00
P B:PTR170 0.0 36.7 1.0
O1P B:PTR170 1.5 35.0 1.0
O3P B:PTR170 1.5 28.0 1.0
O2P B:PTR170 1.5 28.9 1.0
OH B:PTR170 1.8 33.0 1.0
CZ B:PTR170 2.8 33.2 1.0
NH1 A:ARG175 3.2 24.9 1.0
CE1 B:PTR170 3.4 32.2 1.0
NH1 A:ARG195 3.4 10.2 1.0
NH1 A:ARG197 3.6 59.2 1.0
CE2 B:PTR170 3.9 32.7 1.0
NH2 A:ARG195 3.9 7.0 1.0
CZ A:ARG195 4.1 11.4 1.0
CD A:ARG197 4.4 56.8 1.0
CB A:ARG175 4.4 17.1 1.0
CG A:ARG175 4.4 19.1 1.0
CD B:PRO168 4.4 71.7 1.0
CZ A:ARG175 4.4 27.3 1.0
CG A:ARG197 4.6 56.2 1.0
CZ A:ARG197 4.7 59.4 1.0
CD1 B:PTR170 4.7 34.8 1.0
NE A:ARG197 5.0 58.1 1.0

Phosphorus binding site 2 out of 12 in 1a81

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Phosphorus binding site 2 out of 12 in the Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam within 5.0Å range:
probe atom residue distance (Å) B Occ
B:P181

b:24.7
occ:1.00
P B:PTR181 0.0 24.7 1.0
O1P B:PTR181 1.5 22.1 1.0
O3P B:PTR181 1.5 22.8 1.0
OH B:PTR181 1.5 25.1 1.0
O2P B:PTR181 1.5 18.9 1.0
CZ B:PTR181 2.6 27.5 1.0
NH1 A:ARG22 2.9 15.6 1.0
CE1 B:PTR181 3.2 29.6 1.0
CE2 B:PTR181 3.7 23.9 1.0
NH1 A:ARG42 3.7 10.9 1.0
NZ A:LYS232 4.0 44.0 1.0
CB A:ARG22 4.2 12.2 1.0
CZ A:ARG22 4.3 26.4 1.0
NH2 A:ARG42 4.3 13.1 1.0
OD1 A:ASN46 4.4 19.7 1.0
CZ A:ARG42 4.5 8.5 1.0
CD1 B:PTR181 4.5 29.8 1.0
CD2 B:PTR181 4.9 29.3 1.0

Phosphorus binding site 3 out of 12 in 1a81

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Phosphorus binding site 3 out of 12 in the Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 3 of Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam within 5.0Å range:
probe atom residue distance (Å) B Occ
D:P170

b:61.1
occ:1.00
P D:PTR170 0.0 61.1 1.0
O2P D:PTR170 1.5 60.6 1.0
O1P D:PTR170 1.5 57.5 1.0
O3P D:PTR170 1.5 58.1 1.0
OH D:PTR170 1.6 58.1 1.0
CZ D:PTR170 2.7 52.2 1.0
NH1 C:ARG197 3.0 46.8 1.0
CE2 D:PTR170 3.4 46.3 1.0
NH1 C:ARG195 3.5 20.5 1.0
CE1 D:PTR170 3.7 46.4 1.0
NH1 C:ARG175 3.9 73.4 1.0
CZ C:ARG197 3.9 47.4 1.0
NH2 C:ARG197 4.0 41.0 1.0
CB C:ARG175 4.0 55.2 1.0
CD C:ARG175 4.1 64.6 1.0
NH2 C:ARG195 4.4 25.8 1.0
CZ C:ARG195 4.4 22.9 1.0
CD D:PRO168 4.6 67.1 1.0
CD2 D:PTR170 4.6 42.8 1.0
N D:PRO168 4.7 67.5 1.0
CG C:ARG175 4.7 59.7 1.0
CZ C:ARG175 4.9 70.9 1.0
CD1 D:PTR170 4.9 42.3 1.0
NE C:ARG175 5.0 70.2 1.0
NE C:ARG197 5.0 49.2 1.0

Phosphorus binding site 4 out of 12 in 1a81

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Phosphorus binding site 4 out of 12 in the Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 4 of Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam within 5.0Å range:
probe atom residue distance (Å) B Occ
D:P181

b:17.7
occ:1.00
P D:PTR181 0.0 17.7 1.0
O1P D:PTR181 1.5 23.3 1.0
O3P D:PTR181 1.5 6.9 1.0
O2P D:PTR181 1.6 5.4 1.0
OH D:PTR181 1.6 4.7 1.0
CZ D:PTR181 2.6 9.7 1.0
CE2 D:PTR181 3.0 10.9 1.0
NH1 C:ARG42 3.3 4.7 1.0
NH1 C:ARG22 3.5 23.7 1.0
NZ C:LYS232 3.6 29.0 1.0
NH2 C:ARG42 3.8 4.7 1.0
CE1 D:PTR181 3.8 10.7 1.0
CZ C:ARG42 4.0 4.7 1.0
CD2 D:PTR181 4.4 9.8 1.0
CB C:ARG22 4.5 4.7 1.0
CZ C:ARG22 4.8 20.5 1.0
CD C:ARG22 4.9 17.1 1.0
CD1 D:PTR181 5.0 12.8 1.0
CA C:ARG22 5.0 8.8 1.0

Phosphorus binding site 5 out of 12 in 1a81

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Phosphorus binding site 5 out of 12 in the Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 5 of Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam within 5.0Å range:
probe atom residue distance (Å) B Occ
F:P170

b:100.0
occ:1.00
P F:PTR170 0.0 100.0 1.0
O3P F:PTR170 1.5 100.0 1.0
O2P F:PTR170 1.5 100.0 1.0
O1P F:PTR170 1.5 100.0 1.0
OH F:PTR170 1.7 100.0 1.0
CZ F:PTR170 2.8 100.0 1.0
CE1 F:PTR170 3.5 100.0 1.0
CZ E:ARG197 3.5 87.8 1.0
NH1 E:ARG197 3.6 86.2 1.0
NH1 E:ARG195 3.6 53.3 1.0
CE2 F:PTR170 3.7 100.0 1.0
NE E:ARG197 3.7 89.1 1.0
NH2 E:ARG195 3.9 53.7 1.0
NH2 E:ARG197 4.0 85.9 1.0
CD E:ARG197 4.1 87.1 1.0
CZ E:ARG195 4.2 53.6 1.0
NH1 E:ARG175 4.2 94.9 1.0
CB E:ARG175 4.7 69.6 1.0
CD F:PRO168 4.7 91.9 1.0
CD1 F:PTR170 4.7 97.5 1.0
CD E:ARG175 4.8 84.4 1.0
CD2 F:PTR170 4.9 98.8 1.0
N F:PRO168 5.0 94.1 1.0

Phosphorus binding site 6 out of 12 in 1a81

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Phosphorus binding site 6 out of 12 in the Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 6 of Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam within 5.0Å range:
probe atom residue distance (Å) B Occ
F:P181

b:63.2
occ:1.00
P F:PTR181 0.0 63.2 1.0
O2P F:PTR181 1.5 59.8 1.0
O1P F:PTR181 1.5 65.3 1.0
O3P F:PTR181 1.5 59.1 1.0
OH F:PTR181 1.6 61.7 1.0
CZ F:PTR181 2.6 65.4 1.0
CE2 F:PTR181 3.0 64.2 1.0
NH1 E:ARG22 3.3 31.6 1.0
NH1 E:ARG42 3.4 41.0 1.0
CE1 F:PTR181 3.7 66.8 1.0
CB E:ARG22 4.2 9.7 1.0
NH2 E:ARG42 4.3 32.6 1.0
CZ E:ARG42 4.3 38.9 1.0
CD2 F:PTR181 4.3 66.3 1.0
OD1 E:ASN46 4.5 56.4 1.0
CZ E:ARG22 4.5 27.5 1.0
CE E:LYS232 4.8 34.5 1.0
CA E:ARG22 4.8 18.1 1.0
CD1 F:PTR181 4.9 68.8 1.0
N E:ARG22 4.9 17.1 1.0

Phosphorus binding site 7 out of 12 in 1a81

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Phosphorus binding site 7 out of 12 in the Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 7 of Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam within 5.0Å range:
probe atom residue distance (Å) B Occ
H:P170

b:34.6
occ:1.00
P H:PTR170 0.0 34.6 1.0
O1P H:PTR170 1.5 32.2 1.0
O2P H:PTR170 1.5 27.4 1.0
O3P H:PTR170 1.6 25.2 1.0
OH H:PTR170 1.6 34.6 1.0
CZ H:PTR170 2.6 33.8 1.0
NH1 G:ARG197 3.1 32.6 1.0
NH1 G:ARG175 3.2 30.4 1.0
CE2 H:PTR170 3.4 32.3 1.0
CE1 H:PTR170 3.4 30.2 1.0
NH2 A:ARG129 3.6 74.5 1.0
NH1 G:ARG195 3.7 22.5 1.0
CG G:ARG175 3.8 14.8 1.0
NH2 G:ARG195 3.9 24.0 1.0
CZ G:ARG197 4.0 37.9 1.0
NH2 G:ARG197 4.1 37.3 1.0
CB G:ARG175 4.2 18.8 1.0
CZ G:ARG195 4.3 24.4 1.0
CD G:ARG175 4.3 20.1 1.0
CZ G:ARG175 4.4 30.6 1.0
CD2 H:PTR170 4.6 30.5 1.0
CD1 H:PTR170 4.6 29.2 1.0
NE G:ARG175 4.8 29.6 1.0
CD H:PRO168 4.8 81.7 1.0
CZ A:ARG129 4.8 74.5 1.0
N H:PRO168 4.9 80.5 1.0

Phosphorus binding site 8 out of 12 in 1a81

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Phosphorus binding site 8 out of 12 in the Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 8 of Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam within 5.0Å range:
probe atom residue distance (Å) B Occ
H:P181

b:18.0
occ:1.00
P H:PTR181 0.0 18.0 1.0
O1P H:PTR181 1.5 13.4 1.0
O3P H:PTR181 1.5 14.3 1.0
O2P H:PTR181 1.5 11.9 1.0
OH H:PTR181 1.5 15.5 1.0
CZ H:PTR181 2.6 17.8 1.0
CE1 H:PTR181 3.3 19.1 1.0
NH1 G:ARG42 3.3 8.9 1.0
NH1 G:ARG22 3.4 4.7 1.0
CE2 H:PTR181 3.5 15.8 1.0
CB G:ARG22 3.9 6.2 1.0
CZ G:ARG42 4.3 6.5 1.0
NH2 G:ARG42 4.4 4.7 1.0
CD1 H:PTR181 4.6 18.9 1.0
CZ G:ARG22 4.6 13.3 1.0
CD2 H:PTR181 4.7 18.8 1.0
OD1 G:ASN46 4.8 21.6 1.0
CA G:ARG22 4.8 8.1 1.0
CG G:ARG22 4.8 4.7 1.0
N G:ARG22 5.0 4.8 1.0

Phosphorus binding site 9 out of 12 in 1a81

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Phosphorus binding site 9 out of 12 in the Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 9 of Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam within 5.0Å range:
probe atom residue distance (Å) B Occ
J:P170

b:100.0
occ:1.00
P J:PTR170 0.0 100.0 1.0
O2P J:PTR170 1.5 100.0 1.0
O3P J:PTR170 1.5 100.0 1.0
O1P J:PTR170 1.5 100.0 1.0
OH J:PTR170 1.6 100.0 1.0
CZ J:PTR170 2.6 100.0 1.0
CE1 J:PTR170 3.1 100.0 1.0
NH1 I:ARG175 3.4 89.7 1.0
NH1 I:ARG197 3.6 100.0 1.0
CE2 J:PTR170 3.6 100.0 1.0
NH1 I:ARG195 3.6 59.0 1.0
CD I:ARG175 4.1 83.8 1.0
NH2 I:ARG195 4.2 55.9 1.0
CZ I:ARG175 4.2 90.4 1.0
CZ I:ARG195 4.4 60.0 1.0
CD1 J:PTR170 4.4 100.0 1.0
CB I:ARG175 4.4 75.2 1.0
CZ I:ARG197 4.5 100.0 1.0
NE I:ARG175 4.5 88.8 1.0
NH2 I:ARG197 4.6 100.0 1.0
CD J:PRO168 4.6 100.0 1.0
N J:PRO168 4.7 100.0 1.0
CG I:ARG175 4.7 79.1 1.0
CD2 J:PTR170 4.8 100.0 1.0

Phosphorus binding site 10 out of 12 in 1a81

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Phosphorus binding site 10 out of 12 in the Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 10 of Crystal Structure of the Tandem SH2 Domain of the Syk Kinase Bound to A Dually Tyrosine-Phosphorylated Itam within 5.0Å range:
probe atom residue distance (Å) B Occ
J:P181

b:36.1
occ:1.00
P J:PTR181 0.0 36.1 1.0
O1P J:PTR181 1.5 36.2 1.0
OH J:PTR181 1.5 34.5 1.0
O3P J:PTR181 1.5 28.8 1.0
O2P J:PTR181 1.5 30.8 1.0
CZ J:PTR181 2.5 37.5 1.0
NH1 I:ARG22 2.7 16.5 1.0
NH1 I:ARG42 3.1 4.7 1.0
CE2 J:PTR181 3.2 37.2 1.0
CE1 J:PTR181 3.6 41.3 1.0
CB I:ARG22 3.8 6.9 1.0
NH2 I:ARG42 3.8 8.5 1.0
CZ I:ARG42 3.9 7.2 1.0
CZ I:ARG22 3.9 23.1 1.0
CD2 J:PTR181 4.6 40.9 1.0
CA I:ARG22 4.6 7.1 1.0
CD I:ARG22 4.6 16.0 1.0
NE I:ARG22 4.7 22.4 1.0
CG I:ARG22 4.7 4.7 1.0
CD1 J:PTR181 4.8 42.6 1.0
NH2 I:ARG22 4.8 25.8 1.0
N I:ARG22 4.8 4.7 1.0

Reference:

K.Futterer, J.Wong, R.A.Grucza, A.C.Chan, G.Waksman. Structural Basis For Syk Tyrosine Kinase Ubiquity in Signal Transduction Pathways Revealed By the Crystal Structure of Its Regulatory SH2 Domains Bound to A Dually Phosphorylated Itam Peptide. J.Mol.Biol. V. 281 523 1998.
ISSN: ISSN 0022-2836
PubMed: 9698567
DOI: 10.1006/JMBI.1998.1964
Page generated: Fri Sep 25 12:25:47 2020

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