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Cobalt in PDB 9dxu: Crystal Structure of Cobalt-Incorporated Human 2-Aminoethanethiol (Aka Cysteamine) Dioxygenase (Ado) Variant C18S/C239S in Complex with CP6

Enzymatic activity of Crystal Structure of Cobalt-Incorporated Human 2-Aminoethanethiol (Aka Cysteamine) Dioxygenase (Ado) Variant C18S/C239S in Complex with CP6

All present enzymatic activity of Crystal Structure of Cobalt-Incorporated Human 2-Aminoethanethiol (Aka Cysteamine) Dioxygenase (Ado) Variant C18S/C239S in Complex with CP6:
1.13.11.19;

Protein crystallography data

The structure of Crystal Structure of Cobalt-Incorporated Human 2-Aminoethanethiol (Aka Cysteamine) Dioxygenase (Ado) Variant C18S/C239S in Complex with CP6, PDB code: 9dxu was solved by Y.Jiramongkol, K.Patel, M.D.White, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.34 / 1.74
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.111, 71.605, 108.872, 90, 90, 90
R / Rfree (%) 17.5 / 21.5

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Cobalt-Incorporated Human 2-Aminoethanethiol (Aka Cysteamine) Dioxygenase (Ado) Variant C18S/C239S in Complex with CP6 (pdb code 9dxu). 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 Cobalt-Incorporated Human 2-Aminoethanethiol (Aka Cysteamine) Dioxygenase (Ado) Variant C18S/C239S in Complex with CP6, PDB code: 9dxu:

Cobalt binding site 1 out of 1 in 9dxu

Go back to Cobalt Binding Sites List in 9dxu
Cobalt binding site 1 out of 1 in the Crystal Structure of Cobalt-Incorporated Human 2-Aminoethanethiol (Aka Cysteamine) Dioxygenase (Ado) Variant C18S/C239S in Complex with CP6


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 Cobalt-Incorporated Human 2-Aminoethanethiol (Aka Cysteamine) Dioxygenase (Ado) Variant C18S/C239S in Complex with CP6 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co314

b:17.3
occ:1.00
 O A:HOH431 1.9 18.1 0.2
N A:TRS301 1.9 18.2 0.3
N A:TRS301 2.0 14.6 0.3
O3 A:TRS301 2.0 14.8 0.4
NE2 A:HIS112 2.1 11.8 1.0
O A:HOH431 2.1 16.6 0.2
NE2 A:HIS114 2.1 16.4 1.0
NE2 A:HIS193 2.1 17.7 1.0
O1 A:TRS301 2.2 13.8 0.4
C1 A:TRS301 2.3 17.5 0.3
O1 A:TRS301 2.3 18.3 0.3
O2 A:TRS301 2.5 19.9 0.4
O3 A:TRS301 2.5 20.1 0.3
C A:TRS301 2.5 21.5 0.3
C2 A:TRS301 2.5 20.7 0.4
C1 A:TRS301 2.6 21.5 0.4
C A:TRS301 2.6 21.7 0.4
C3 A:TRS301 2.7 20.5 0.4
CE1 A:HIS112 3.0 14.9 1.0
C A:TRS301 3.0 18.2 0.3
CE1 A:HIS193 3.1 16.9 1.0
O A:HOH431 3.1 15.8 0.2
CE1 A:HIS114 3.1 17.5 1.0
CD2 A:HIS112 3.1 18.0 1.0
CD2 A:HIS193 3.1 19.7 1.0
CD2 A:HIS114 3.2 16.7 1.0
O3 A:TRS301 3.3 15.7 0.3
C3 A:TRS301 3.3 17.8 0.3
C3 A:TRS301 3.4 18.9 0.3
O2 A:TRS301 3.6 20.2 0.3
C2 A:TRS301 3.6 18.3 0.3
C2 A:TRS301 3.8 23.1 0.3
O A:HOH431 4.0 21.1 0.5
N A:TRS301 4.1 18.1 0.4
ND1 A:HIS112 4.1 14.7 1.0
ND1 A:HIS193 4.2 20.6 1.0
ND1 A:HIS114 4.2 18.3 1.0
CG A:HIS112 4.2 13.8 1.0
CG A:HIS193 4.2 19.3 1.0
C1 A:TRS301 4.3 14.4 0.3
CG A:HIS114 4.3 19.1 1.0
OH A:TYR212 4.5 18.9 1.0
O1 A:TRS301 4.6 26.0 0.3
O2 A:TRS301 4.7 25.7 0.3
O A:HOH501 4.8 35.8 1.0
CD1 A:ILE195 4.9 25.1 1.0
CD2 A:LEU185 4.9 21.7 1.0

Reference:

Y.Jiramongkol, K.Patel, J.Johansen-Leete, J.W.C.Maxwell, Y.Chang, J.J.Du, T.Passioura, K.M.Cook, R.J.Payne, M.D.White. An Mrna-Display Derived Cyclic Peptide Scaffold Reveals the Substrate Binding Interactions of An N-Terminal Cysteine Oxidase. Nat Commun V. 16 4761 2025.
ISSN: ESSN 2041-1723
PubMed: 40404614
DOI: 10.1038/S41467-025-59960-3
Page generated: Sun Jul 13 22:13:02 2025

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