Phosphorus in PDB 1agp: Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras

Protein crystallography data

The structure of Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras, PDB code: 1agp was solved by S.M.Franken, A.J.Scheidig, A.Wittinghofer, R.S.Goody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 69.910, 39.810, 56.100, 90.00, 107.40, 90.00
R / Rfree (%) 17.7 / n/a

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras (pdb code 1agp). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 3 binding sites of Phosphorus where determined in the Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras, PDB code: 1agp:
Jump to Phosphorus binding site number: 1; 2; 3;

Phosphorus binding site 1 out of 3 in 1agp

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Phosphorus binding site 1 out of 3 in the Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P167

b:7.6
occ:1.00
PG A:GNP167 0.0 7.6 1.0
O1G A:GNP167 1.5 5.6 1.0
O3G A:GNP167 1.5 9.8 1.0
O2G A:GNP167 1.6 9.8 1.0
N3B A:GNP167 1.7 5.5 1.0
HOG2 A:GNP167 2.1 0.0 1.0
HNB3 A:GNP167 2.2 0.0 1.0
HZ2 A:LYS16 2.8 0.0 1.0
PB A:GNP167 2.8 3.3 1.0
H2 A:HOH172 2.9 0.0 1.0
H A:THR35 3.1 0.0 1.0
H A:GLY60 3.2 0.0 1.0
H A:GLY13 3.2 0.0 1.0
O2B A:GNP167 3.3 4.0 1.0
OD1 A:ASP12 3.4 21.6 1.0
O A:HOH172 3.5 4.6 1.0
O1B A:GNP167 3.5 4.5 1.0
MG A:MG168 3.5 6.9 1.0
NZ A:LYS16 3.8 2.6 1.0
HZ3 A:LYS16 4.0 0.0 1.0
N A:GLY60 4.1 9.4 1.0
N A:THR35 4.1 12.7 1.0
N A:GLY13 4.1 2.1 1.0
O3A A:GNP167 4.2 5.0 1.0
H1 A:HOH172 4.2 0.0 1.0
HZ1 A:LYS16 4.3 0.0 1.0
CA A:ASP12 4.4 8.2 1.0
CG A:ASP12 4.5 18.6 1.0
CA A:PRO34 4.5 10.3 1.0
CE A:LYS16 4.6 2.0 1.0
HH A:TYR32 4.7 0.0 1.0
O2A A:GNP167 4.7 11.8 1.0
CA A:GLY60 4.7 9.7 1.0
OG1 A:THR35 4.7 10.8 1.0
H A:GLN61 4.7 0.0 1.0
CE1 A:TYR32 4.7 14.5 1.0
C A:ASP12 4.7 4.6 1.0
HG A:SER17 4.8 0.0 1.0
C A:PRO34 4.8 9.7 1.0
O A:THR58 4.8 9.3 1.0
CB A:ASP12 5.0 13.0 1.0
CB A:THR35 5.0 12.6 1.0

Phosphorus binding site 2 out of 3 in 1agp

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Phosphorus binding site 2 out of 3 in the Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P167

b:3.3
occ:1.00
PB A:GNP167 0.0 3.3 1.0
O2B A:GNP167 1.5 4.0 1.0
O1B A:GNP167 1.5 4.5 1.0
O3A A:GNP167 1.6 5.0 1.0
N3B A:GNP167 1.7 5.5 1.0
HNB3 A:GNP167 2.2 0.0 1.0
PG A:GNP167 2.8 7.6 1.0
PA A:GNP167 2.9 3.5 1.0
HZ2 A:LYS16 3.0 0.0 1.0
H2 A:HOH172 3.0 0.0 1.0
H A:LYS16 3.0 0.0 1.0
H A:GLY13 3.1 0.0 1.0
H A:GLY15 3.1 0.0 1.0
O2A A:GNP167 3.2 11.8 1.0
H A:SER17 3.2 0.0 1.0
O1G A:GNP167 3.3 5.6 1.0
O A:HOH172 3.4 4.6 1.0
O3G A:GNP167 3.5 9.8 1.0
HZ1 A:LYS16 3.6 0.0 1.0
MG A:MG168 3.6 6.9 1.0
O1A A:GNP167 3.6 5.2 1.0
NZ A:LYS16 3.7 2.6 1.0
N A:LYS16 3.8 7.1 1.0
HG A:SER17 3.8 0.0 1.0
N A:GLY13 3.9 2.1 1.0
N A:GLY15 4.0 5.6 1.0
O5' A:GNP167 4.1 8.3 1.0
O2G A:GNP167 4.1 9.8 1.0
N A:SER17 4.2 10.3 1.0
H5'1 A:GNP167 4.2 0.0 1.0
CA A:GLY13 4.2 2.0 1.0
HOG2 A:GNP167 4.2 0.0 1.0
H1 A:HOH172 4.2 0.0 1.0
H A:VAL14 4.3 0.0 1.0
CB A:LYS16 4.3 4.7 1.0
CA A:GLY15 4.4 6.5 1.0
C A:GLY13 4.4 4.6 1.0
OG A:SER17 4.4 3.3 1.0
HZ3 A:LYS16 4.4 0.0 1.0
CG A:LYS16 4.4 6.7 1.0
N A:VAL14 4.4 6.3 1.0
C A:GLY15 4.5 6.2 1.0
CA A:LYS16 4.5 8.2 1.0
CD A:LYS16 4.5 7.0 1.0
C5' A:GNP167 4.5 9.2 1.0
H5'2 A:GNP167 4.6 0.0 1.0
CE A:LYS16 4.7 2.0 1.0
C A:LYS16 4.9 10.2 1.0
H A:ALA18 4.9 0.0 1.0
O A:ALA11 4.9 12.9 1.0
O A:GLY13 5.0 6.1 1.0

Phosphorus binding site 3 out of 3 in 1agp

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Phosphorus binding site 3 out of 3 in the Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 3 of Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P167

b:3.5
occ:1.00
PA A:GNP167 0.0 3.5 1.0
O1A A:GNP167 1.5 5.2 1.0
O2A A:GNP167 1.5 11.8 1.0
O5' A:GNP167 1.6 8.3 1.0
O3A A:GNP167 1.6 5.0 1.0
C5' A:GNP167 2.6 9.2 1.0
H5'2 A:GNP167 2.8 0.0 1.0
PB A:GNP167 2.9 3.3 1.0
H5'1 A:GNP167 3.0 0.0 1.0
O2B A:GNP167 3.1 4.0 1.0
HNB3 A:GNP167 3.3 0.0 1.0
H A:SER17 3.5 0.0 1.0
H2 A:HOH172 3.5 0.0 1.0
H A:GLY15 3.6 0.0 1.0
H2' A:GNP167 3.6 0.0 1.0
H A:ALA18 3.7 0.0 1.0
N3B A:GNP167 3.7 5.5 1.0
H8 A:GNP167 3.7 0.0 1.0
HG A:SER17 3.8 0.0 1.0
O A:HOH172 3.9 4.6 1.0
CA A:GLY15 3.9 6.5 1.0
C4' A:GNP167 3.9 7.9 1.0
O1B A:GNP167 4.0 4.5 1.0
H3' A:GNP167 4.0 0.0 1.0
N A:GLY15 4.1 5.6 1.0
H A:LYS16 4.1 0.0 1.0
H1 A:HOH172 4.1 0.0 1.0
N A:SER17 4.3 10.3 1.0
O4' A:GNP167 4.3 8.7 1.0
C A:GLY15 4.4 6.2 1.0
C3' A:GNP167 4.4 9.7 1.0
N A:LYS16 4.4 7.1 1.0
CB A:SER17 4.4 7.7 1.0
C2' A:GNP167 4.5 9.8 1.0
OG A:SER17 4.5 3.3 1.0
N A:ALA18 4.5 2.9 1.0
CB A:ALA18 4.6 4.0 1.0
C8 A:GNP167 4.7 5.9 1.0
H4' A:GNP167 4.8 0.0 1.0
CA A:SER17 4.9 9.0 1.0
O A:GLY13 4.9 6.1 1.0
C1' A:GNP167 5.0 7.2 1.0

Reference:

S.M.Franken, A.J.Scheidig, U.Krengel, H.Rensland, A.Lautwein, M.Geyer, K.Scheffzek, R.S.Goody, H.R.Kalbitzer, E.F.Pai, A.Wittinghofer. Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Glycine-12 Mutant of P21H-Ras. Biochemistry V. 32 8411 1993.
ISSN: ISSN 0006-2960
PubMed: 8357792
DOI: 10.1021/BI00084A005
Page generated: Fri Sep 25 12:53:24 2020

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