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Cobalt in PDB 1s3h: Propionibacterium Shermanii Transcarboxylase 5S Subunit A59T

Enzymatic activity of Propionibacterium Shermanii Transcarboxylase 5S Subunit A59T

All present enzymatic activity of Propionibacterium Shermanii Transcarboxylase 5S Subunit A59T:
2.1.3.1;

Protein crystallography data

The structure of Propionibacterium Shermanii Transcarboxylase 5S Subunit A59T, PDB code: 1s3h 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) 29.19 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 96.258, 146.320, 78.718, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 25

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Propionibacterium Shermanii Transcarboxylase 5S Subunit A59T (pdb code 1s3h). 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 A59T, PDB code: 1s3h:

Cobalt binding site 1 out of 1 in 1s3h

Go back to Cobalt Binding Sites List in 1s3h
Cobalt binding site 1 out of 1 in the Propionibacterium Shermanii Transcarboxylase 5S Subunit A59T


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 A59T within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co529

b:29.9
occ:1.00
OD1 A:ASP23 2.0 13.6 1.0
OQ2 A:KCX184 2.1 26.5 1.0
NE2 A:HIS215 2.2 8.9 1.0
OQ1 A:KCX184 2.2 29.1 1.0
NE2 A:HIS217 2.2 5.5 1.0
CX A:KCX184 2.5 26.8 1.0
CG A:ASP23 3.0 12.7 1.0
CE1 A:HIS215 3.1 9.8 1.0
CD2 A:HIS215 3.1 8.9 1.0
CE1 A:HIS217 3.1 5.5 1.0
CD2 A:HIS217 3.2 5.5 1.0
OD2 A:ASP23 3.3 14.0 1.0
NE2 A:HIS251 3.8 5.5 1.0
NZ A:KCX184 3.8 25.1 1.0
ND1 A:HIS215 4.2 9.0 1.0
CG A:HIS215 4.3 9.3 1.0
ND1 A:HIS217 4.3 5.5 1.0
NH2 A:ARG22 4.3 12.4 1.0
CB A:ASP23 4.3 10.7 1.0
O A:HOH530 4.4 13.8 1.0
CG A:HIS217 4.4 6.7 1.0
CE A:MET186 4.4 27.8 1.0
CD2 A:HIS251 4.6 5.9 1.0
CG A:MET186 4.7 23.5 1.0
CE1 A:HIS251 4.8 5.5 1.0
CE A:KCX184 4.8 23.7 1.0
CA A:MET186 4.8 14.4 1.0
CB A:MET186 4.9 18.2 1.0
OG A:SER27 5.0 8.2 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: Sun Jul 13 17:47:10 2025

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