Cobalt in PDB 1rqe: Propionibacterium Shermanii Transcarboxylase 5S Subunit Bound to Oxaloacetate

All present enzymatic activity of Propionibacterium Shermanii Transcarboxylase 5S Subunit Bound to Oxaloacetate:
2.1.3.1;

The structure of Propionibacterium Shermanii Transcarboxylase 5S Subunit Bound to Oxaloacetate, PDB code: 1rqe 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)	27.17 / 2.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	95.865, 145.488, 78.192, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 22.6

The binding sites of Cobalt atom in the Propionibacterium Shermanii Transcarboxylase 5S Subunit Bound to Oxaloacetate (pdb code 1rqe). 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 Bound to Oxaloacetate, PDB code: 1rqe:

Cobalt binding site 1 out of 1 in the Propionibacterium Shermanii Transcarboxylase 5S Subunit Bound to Oxaloacetate


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 Bound to Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ A:Co530 b:21.1 occ:1.00 O1 A:OAA529 1.7 31.0 0.8 OD1 A:ASP23 1.9 27.0 1.0 NE2 A:HIS215 2.0 10.8 1.0 NE2 A:HIS217 2.0 11.3 1.0 C1 A:OAA529 2.7 29.9 0.8 CG A:ASP23 2.9 21.9 1.0 CE1 A:HIS217 3.0 10.5 1.0 CE1 A:HIS215 3.0 10.2 1.0 O2 A:OAA529 3.0 23.8 0.8 CD2 A:HIS215 3.0 14.3 1.0 CD2 A:HIS217 3.1 11.3 1.0 OD2 A:ASP23 3.3 20.7 1.0 NE2 A:HIS251 3.9 14.2 1.0 C2 A:OAA529 4.1 33.1 0.8 ND1 A:HIS215 4.1 10.1 1.0 ND1 A:HIS217 4.1 11.1 1.0 CG A:HIS215 4.2 10.2 1.0 CG A:HIS217 4.2 14.1 1.0 CB A:ASP23 4.3 18.8 1.0 O3 A:OAA529 4.3 32.6 0.8 NH2 A:ARG22 4.4 11.4 1.0 O A:HOH571 4.4 23.3 1.0 CE A:MET186 4.4 11.2 0.2 CD2 A:HIS251 4.6 16.5 1.0 C3 A:OAA529 4.7 35.7 0.8 CA A:MET186 4.8 20.2 1.0 CG A:MET186 4.8 15.9 0.2 CB A:MET186 4.8 16.6 0.2 CG A:MET186 4.9 37.4 0.8 CB A:MET186 4.9 26.0 0.8 CE1 A:HIS251 4.9 15.2 1.0

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