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Cobalt in PDB 1xrs: Crystal Structure of Lysine 5,6-Aminomutase in Complex with Plp, Cobalamin, and 5'-Deoxyadenosine

Enzymatic activity of Crystal Structure of Lysine 5,6-Aminomutase in Complex with Plp, Cobalamin, and 5'-Deoxyadenosine

All present enzymatic activity of Crystal Structure of Lysine 5,6-Aminomutase in Complex with Plp, Cobalamin, and 5'-Deoxyadenosine:
5.4.3.3;

Protein crystallography data

The structure of Crystal Structure of Lysine 5,6-Aminomutase in Complex with Plp, Cobalamin, and 5'-Deoxyadenosine, PDB code: 1xrs was solved by F.Berkovitch, E.Behshad, K.H.Tang, E.A.Enns, P.A.Frey, C.L.Drennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.85 / 2.80
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 99.700, 99.700, 168.800, 90.00, 90.00, 120.00
R / Rfree (%) 19.9 / 26.2

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Lysine 5,6-Aminomutase in Complex with Plp, Cobalamin, and 5'-Deoxyadenosine (pdb code 1xrs). 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 Lysine 5,6-Aminomutase in Complex with Plp, Cobalamin, and 5'-Deoxyadenosine, PDB code: 1xrs:

Cobalt binding site 1 out of 1 in 1xrs

Go back to Cobalt Binding Sites List in 1xrs
Cobalt binding site 1 out of 1 in the Crystal Structure of Lysine 5,6-Aminomutase in Complex with Plp, Cobalamin, and 5'-Deoxyadenosine


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 Lysine 5,6-Aminomutase in Complex with Plp, Cobalamin, and 5'-Deoxyadenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co800

b:0.9
occ:1.00
 CO B:B12800 0.0 0.9 1.0
N21 B:B12800 1.9 27.1 1.0
N24 B:B12800 1.9 24.0 1.0
N23 B:B12800 2.0 24.9 1.0
N22 B:B12800 2.0 25.2 1.0
NE2 B:HIS133 2.5 32.4 1.0
C5' B:5AD500 2.6 81.4 1.0
C19 B:B12800 2.7 34.2 1.0
C1 B:B12800 2.7 36.3 1.0
C4 B:B12800 2.9 29.8 1.0
C9 B:B12800 2.9 25.9 1.0
C16 B:B12800 2.9 32.8 1.0
C6 B:B12800 2.9 30.9 1.0
C11 B:B12800 2.9 23.9 1.0
C14 B:B12800 3.0 26.0 1.0
C10 B:B12800 3.3 22.5 1.0
CE1 B:HIS133 3.3 31.3 1.0
C5 B:B12800 3.3 35.5 1.0
C20 B:B12800 3.4 35.1 1.0
C15 B:B12800 3.4 26.0 1.0
CD2 B:HIS133 3.6 30.1 1.0
C4' B:5AD500 3.8 79.9 1.0
C18 B:B12800 3.9 36.0 1.0
C2 B:B12800 4.1 36.2 1.0
C8 B:B12800 4.1 28.1 1.0
C17 B:B12800 4.2 35.0 1.0
C7 B:B12800 4.2 33.5 1.0
C3 B:B12800 4.2 31.5 1.0
O4' B:5AD500 4.3 83.6 1.0
C13 B:B12800 4.3 24.9 1.0
C12 B:B12800 4.3 27.8 1.0
ND1 B:HIS133 4.5 26.6 1.0
C37 B:B12800 4.6 41.8 1.0
CG B:HIS133 4.7 27.9 1.0
C26 B:B12800 4.7 41.7 1.0
C35 B:B12800 4.8 43.8 1.0
C53 B:B12800 4.8 24.2 1.0
C41 B:B12800 4.8 25.3 1.0
C46 B:B12800 4.9 23.4 1.0

Reference:

F.Berkovitch, E.Behshad, K.H.Tang, E.A.Enns, P.A.Frey, C.L.Drennan. A Locking Mechanism Preventing Radical Damage in the Absence of Substrate, As Revealed By the X-Ray Structure of Lysine 5,6-Aminomutase. Proc.Natl.Acad.Sci.Usa V. 101 15870 2004.
ISSN: ISSN 0027-8424
PubMed: 15514022
DOI: 10.1073/PNAS.0407074101
Page generated: Sun Jul 13 17:56:42 2025

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