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Cobalt in PDB 2xwp: Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole

Enzymatic activity of Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole

All present enzymatic activity of Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole:
4.99.1.3;

Protein crystallography data

The structure of Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole, PDB code: 2xwp was solved by D.Ladakis, A.A.Brindley, E.Deery, M.J.Warren, R.W.Pickersgill, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.77 / 1.90
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 110.630, 110.630, 89.530, 90.00, 90.00, 120.00
R / Rfree (%) 19.4 / 23.9

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole (pdb code 2xwp). 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 Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole, PDB code: 2xwp:

Cobalt binding site 1 out of 1 in 2xwp

Go back to Cobalt Binding Sites List in 2xwp
Cobalt binding site 1 out of 1 in the Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co1259

b:23.5
occ:1.00
 CO A:SIR1259 0.0 23.5 1.0
ND A:SIR1259 1.9 19.6 1.0
NA A:SIR1259 1.9 26.1 1.0
NC A:SIR1259 1.9 25.9 1.0
NB A:SIR1259 1.9 27.7 1.0
CHB A:SIR1259 2.8 28.1 1.0
C4A A:SIR1259 2.9 24.7 1.0
C1A A:SIR1259 2.9 28.8 1.0
C4B A:SIR1259 2.9 31.2 1.0
C1C A:SIR1259 2.9 25.9 1.0
C1B A:SIR1259 2.9 29.2 1.0
C4D A:SIR1259 3.0 24.1 1.0
C1D A:SIR1259 3.0 20.4 1.0
C4C A:SIR1259 3.0 21.3 1.0
CZ A:PHE10 3.3 22.7 1.0
CHC A:SIR1259 3.3 25.7 1.0
CE1 A:HIS145 3.3 22.7 0.5
CHA A:SIR1259 3.3 24.7 1.0
CHD A:SIR1259 3.3 17.6 1.0
O A:HOH2143 3.4 16.5 0.3
NE2 A:HIS145 3.6 20.1 0.5
CE1 A:PHE10 3.6 19.0 1.0
CE1 A:HIS145 3.6 19.9 0.5
NE2 A:HIS145 3.6 20.4 0.5
ND1 A:HIS145 3.9 21.4 0.5
O A:HOH2096 4.1 32.2 0.7
CE2 A:PHE10 4.1 22.9 1.0
CD2 A:HIS145 4.1 20.6 0.5
C3D A:SIR1259 4.2 20.7 1.0
C2C A:SIR1259 4.2 27.9 1.0
ND1 A:HIS145 4.2 19.2 0.5
C2D A:SIR1259 4.2 20.6 1.0
C3B A:SIR1259 4.2 34.4 1.0
C3C A:SIR1259 4.2 22.9 1.0
C2A A:SIR1259 4.2 30.7 1.0
C3A A:SIR1259 4.3 27.2 1.0
C2B A:SIR1259 4.3 34.5 1.0
CD2 A:HIS145 4.4 20.4 0.5
CG A:HIS145 4.5 16.8 0.5
CG A:HIS145 4.5 18.1 0.5
O4A A:SIR1259 4.6 51.9 1.0
CD1 A:PHE10 4.6 16.4 1.0
CDA A:SIR1259 4.8 39.0 1.0
CAA A:SIR1259 4.9 28.5 1.0
CMB A:SIR1259 5.0 32.6 1.0

Reference:

C.V.Romao, D.Ladakis, S.A.Lobo, M.A.Carrondo, A.A.Brindley, E.Deery, P.M.Matias, R.W.Pickersgill, L.M.Saraiva, M.J.Warren. Evolution in A Family of Chelatases Facilitated By the Introduction of Active Site Asymmetry and Protein Oligomerization. Proc.Natl.Acad.Sci.Usa V. 108 97 2011.
ISSN: ISSN 0027-8424
PubMed: 21173279
DOI: 10.1073/PNAS.1014298108
Page generated: Sun Jul 13 18:37:59 2025

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