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Nickel in PDB 3gc8: The Structure of P38BETA C162S in Complex with A Dihydroquinazolinone

Enzymatic activity of The Structure of P38BETA C162S in Complex with A Dihydroquinazolinone

All present enzymatic activity of The Structure of P38BETA C162S in Complex with A Dihydroquinazolinone:
2.7.11.24;

Protein crystallography data

The structure of The Structure of P38BETA C162S in Complex with A Dihydroquinazolinone, PDB code: 3gc8 was solved by G.Scapin, S.B.Patel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.124, 157.710, 60.360, 90.00, 91.57, 90.00
R / Rfree (%) 20.8 / 27.2

Other elements in 3gc8:

The structure of The Structure of P38BETA C162S in Complex with A Dihydroquinazolinone also contains other interesting chemical elements:

Fluorine (F) 2 atoms
Chlorine (Cl) 6 atoms
Sodium (Na) 2 atoms

Nickel Binding Sites:

The binding sites of Nickel atom in the The Structure of P38BETA C162S in Complex with A Dihydroquinazolinone (pdb code 3gc8). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the The Structure of P38BETA C162S in Complex with A Dihydroquinazolinone, PDB code: 3gc8:

Nickel binding site 1 out of 1 in 3gc8

Go back to Nickel Binding Sites List in 3gc8
Nickel binding site 1 out of 1 in the The Structure of P38BETA C162S in Complex with A Dihydroquinazolinone


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of The Structure of P38BETA C162S in Complex with A Dihydroquinazolinone within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ni602

b:24.9
occ:1.00
 OE2 B:GLU245 1.9 23.3 1.0
OD1 B:ASP294 1.9 25.3 1.0
OD2 B:ASP292 1.9 27.6 1.0
NE2 A:HIS199 2.1 21.6 1.0
CD B:GLU245 2.7 24.9 1.0
CG B:ASP292 2.8 26.5 1.0
CG B:ASP294 2.8 24.9 1.0
OE1 B:GLU245 3.0 24.6 1.0
CE1 A:HIS199 3.0 20.9 1.0
OD1 B:ASP292 3.0 26.3 1.0
OD2 B:ASP294 3.0 25.2 1.0
CD2 A:HIS199 3.1 22.3 1.0
CG B:GLN295 4.1 28.5 1.0
ND1 A:HIS199 4.1 22.4 1.0
NZ B:LYS249 4.1 39.9 1.0
CG B:GLU245 4.2 23.7 1.0
CB B:ASP292 4.2 25.6 1.0
CB B:ASP294 4.2 24.3 1.0
CG A:HIS199 4.2 24.0 1.0
NE2 B:GLN295 4.3 29.4 1.0
CB A:MET198 4.3 29.8 1.0
O B:HOH445 4.4 19.6 1.0
CD B:GLN295 4.6 30.9 1.0
C B:ASP294 4.6 26.5 1.0
O B:HOH516 4.6 35.8 1.0
CA B:ASP294 4.7 25.5 1.0
N B:ASP294 4.7 24.5 1.0
CG A:MET198 4.7 33.9 1.0
N B:GLN295 4.8 27.6 1.0
CE B:LYS249 4.8 39.4 1.0
O B:ASP294 5.0 27.0 1.0

Reference:

S.B.Patel, P.M.Cameron, S.J.O'keefe, B.Frantz-Wattley, J.Thompson, E.A.O'neill, T.Tennis, L.Liu, J.W.Becker, G.Scapin. The Three-Dimensional Structure of Map Kinase P38BETA: Different Features of the Atp-Binding Site in P38BETA Compared with P38ALPHA. Acta Crystallogr.,Sect.D V. 65 777 2009.
ISSN: ISSN 0907-4449
PubMed: 19622861
DOI: 10.1107/S090744490901600X
Page generated: Mon Aug 18 18:37:44 2025

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