Phosphorus in PDB 1a2q: Subtilisin Bpn' Mutant 7186

Enzymatic activity of Subtilisin Bpn' Mutant 7186

All present enzymatic activity of Subtilisin Bpn' Mutant 7186:
3.4.21.62;

Protein crystallography data

The structure of Subtilisin Bpn' Mutant 7186, PDB code: 1a2q was solved by G.L.Gilliland, M.Whitlow, A.J.Howard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.640, 79.450, 37.260, 90.00, 114.53, 90.00
R / Rfree (%) n/a / n/a

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the Subtilisin Bpn' Mutant 7186 (pdb code 1a2q). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total only one binding site of Phosphorus was determined in the Subtilisin Bpn' Mutant 7186, PDB code: 1a2q:

Phosphorus binding site 1 out of 1 in 1a2q

Go back to Phosphorus Binding Sites List in 1a2q
Phosphorus binding site 1 out of 1 in the Subtilisin Bpn' Mutant 7186


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Subtilisin Bpn' Mutant 7186 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P221

b:11.8
occ:1.00
P A:MIS221 0.0 11.8 1.0
O2P A:MIS221 1.4 9.7 1.0
O1P A:MIS221 1.4 13.8 1.0
O3P A:MIS221 1.5 13.6 1.0
OG A:MIS221 1.6 8.1 1.0
C1 A:MIS221 2.6 15.8 1.0
CB A:MIS221 2.6 6.9 1.0
C2 A:MIS221 3.3 15.7 1.0
O A:HOH463 3.4 12.8 0.3
N A:MIS221 3.5 5.3 1.0
CA A:MIS221 3.5 6.0 1.0
ND2 A:ASN155 3.6 8.9 1.0
C3 A:MIS221 3.8 18.2 1.0
N A:THR220 4.5 6.2 1.0
CG A:ASN155 4.6 8.1 1.0
C A:THR220 4.7 5.4 1.0
O A:SER125 4.7 11.7 1.0
CA A:GLY219 4.7 6.8 1.0
C A:MIS221 4.8 6.1 1.0
O A:HOH281 4.8 16.0 1.0
C A:GLY219 4.8 7.1 1.0
OD1 A:ASN155 4.8 8.3 1.0
OG1 A:THR220 4.8 5.6 1.0
O A:HOH447 5.0 13.7 0.5

Reference:

M.W.Pantoliano, M.Whitlow, J.F.Wood, S.W.Dodd, K.D.Hardman, M.L.Rollence, P.N.Bryan. Large Increases in General Stability For Subtilisin Bpn' Through Incremental Changes in the Free Energy of Unfolding. Biochemistry V. 28 7205 1989.
ISSN: ISSN 0006-2960
PubMed: 2684274
DOI: 10.1021/BI00444A012
Page generated: Fri Sep 25 12:04:14 2020

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