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Cobalt in PDB 1u5j: Propionibacterium Shermanii Transcarboxylase 5S Subunit, MET186ILE

Enzymatic activity of Propionibacterium Shermanii Transcarboxylase 5S Subunit, MET186ILE

All present enzymatic activity of Propionibacterium Shermanii Transcarboxylase 5S Subunit, MET186ILE:
2.1.3.1;

Protein crystallography data

The structure of Propionibacterium Shermanii Transcarboxylase 5S Subunit, MET186ILE, PDB code: 1u5j was solved by P.R.Hall, R.Zheng, L.Antony, M.Pusztai-Carey, P.R.Carey, V.C.Yee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.24 / 2.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 95.680, 147.042, 78.812, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 26.8

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Propionibacterium Shermanii Transcarboxylase 5S Subunit, MET186ILE (pdb code 1u5j). 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 Propionibacterium Shermanii Transcarboxylase 5S Subunit, MET186ILE, PDB code: 1u5j:

Cobalt binding site 1 out of 1 in 1u5j

Go back to Cobalt Binding Sites List in 1u5j
Cobalt binding site 1 out of 1 in the Propionibacterium Shermanii Transcarboxylase 5S Subunit, MET186ILE


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Propionibacterium Shermanii Transcarboxylase 5S Subunit, MET186ILE within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co529

b:36.3
occ:1.00
OQ2 A:KCX184 1.5 48.9 1.0
OD1 A:ASP23 2.0 29.8 1.0
NE2 A:HIS215 2.0 16.1 1.0
NE2 A:HIS217 2.2 17.4 1.0
CX A:KCX184 2.3 45.9 1.0
OQ1 A:KCX184 2.7 43.4 1.0
O A:HOH557 2.8 23.0 1.0
CE1 A:HIS215 2.9 15.7 1.0
CG A:ASP23 3.0 28.4 1.0
CE1 A:HIS217 3.1 20.2 1.0
CD2 A:HIS215 3.1 15.1 1.0
CD2 A:HIS217 3.2 17.9 1.0
OD2 A:ASP23 3.4 30.2 1.0
NZ A:KCX184 3.5 46.7 1.0
NE2 A:HIS251 3.9 31.1 1.0
ND1 A:HIS215 4.0 16.5 1.0
CG A:HIS215 4.2 17.7 1.0
ND1 A:HIS217 4.2 16.6 1.0
CG A:HIS217 4.3 17.9 1.0
CB A:ASP23 4.3 23.7 1.0
NH2 A:ARG22 4.4 21.7 1.0
O A:HOH533 4.4 31.3 1.0
CD2 A:HIS251 4.5 27.1 1.0
CG1 A:ILE186 4.6 31.4 1.0
CE A:KCX184 4.7 44.6 1.0
CB A:ILE186 4.7 28.2 1.0
CA A:ILE186 4.9 24.6 1.0

Reference:

P.R.Hall, R.Zheng, L.Antony, M.Pusztai-Carey, P.R.Carey, V.C.Yee. Transcarboxylase 5S Structures: Assembly and Catalytic Mechanism of A Multienzyme Complex Subunit. Embo J. V. 23 3621 2004.
ISSN: ISSN 0261-4189
PubMed: 15329673
DOI: 10.1038/SJ.EMBOJ.7600373
Page generated: Tue Jul 30 14:39:03 2024

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