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Cobalt in PDB 1diy: Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Active Site of Pghs-1

Enzymatic activity of Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Active Site of Pghs-1

All present enzymatic activity of Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Active Site of Pghs-1:
1.14.99.1;

Protein crystallography data

The structure of Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Active Site of Pghs-1, PDB code: 1diy was solved by M.G.Malkowski, S.L.Ginell, W.L.Smith, R.M.Garavito, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 9.00 / 3.00
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 182.100, 182.100, 103.640, 90.00, 90.00, 120.00
R / Rfree (%) 21.5 / 29

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Active Site of Pghs-1 (pdb code 1diy). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Active Site of Pghs-1, PDB code: 1diy:

Cobalt binding site 1 out of 1 in 1diy

Go back to Cobalt Binding Sites List in 1diy
Cobalt binding site 1 out of 1 in the Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Active Site of Pghs-1


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of Arachidonic Acid Bound in the Cyclooxygenase Active Site of Pghs-1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co601

b:74.8
occ:1.00
CO A:COH601 0.0 74.8 1.0
ND A:COH601 1.9 74.8 1.0
NB A:COH601 2.0 74.8 1.0
NA A:COH601 2.0 74.8 1.0
NC A:COH601 2.0 74.8 1.0
NE2 A:HIS388 2.2 61.0 1.0
C4D A:COH601 3.0 74.8 1.0
C1C A:COH601 3.0 74.8 1.0
C4B A:COH601 3.0 74.8 1.0
C1A A:COH601 3.0 74.8 1.0
C1D A:COH601 3.0 74.8 1.0
C4A A:COH601 3.1 74.8 1.0
C1B A:COH601 3.1 74.8 1.0
C4C A:COH601 3.1 74.8 1.0
CE1 A:HIS388 3.1 61.0 1.0
CD2 A:HIS388 3.3 61.0 1.0
CHA A:COH601 3.3 74.8 1.0
CHC A:COH601 3.3 74.8 1.0
CHB A:COH601 3.4 74.8 1.0
CHD A:COH601 3.4 74.8 1.0
OE1 A:GLN203 4.2 45.8 1.0
C3D A:COH601 4.3 74.8 1.0
ND1 A:HIS388 4.3 61.0 1.0
C2C A:COH601 4.3 74.8 1.0
C3C A:COH601 4.3 74.8 1.0
C3B A:COH601 4.3 74.8 1.0
C2B A:COH601 4.3 74.8 1.0
C2D A:COH601 4.3 74.8 1.0
C2A A:COH601 4.4 74.8 1.0
CG A:HIS388 4.4 61.0 1.0
C3A A:COH601 4.4 74.8 1.0
CG1 A:VAL447 4.5 35.8 1.0
CG2 A:VAL447 4.7 35.8 1.0
CE1 A:HIS207 4.9 47.3 1.0
NE2 A:HIS207 5.0 47.3 1.0

Reference:

M.G.Malkowski, S.L.Ginell, W.L.Smith, R.M.Garavito. The Productive Conformation of Arachidonic Acid Bound to Prostaglandin Synthase. Science V. 289 1933 2000.
ISSN: ISSN 0036-8075
PubMed: 10988074
DOI: 10.1126/SCIENCE.289.5486.1933
Page generated: Sun Jul 13 17:26:47 2025

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