2DJ5
Crystal Structure of the vitamin B12 biosynthetic cobaltochelatase, CbiXS, from Archaeoglobus fulgidus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009236 | biological_process | cobalamin biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0016852 | molecular_function | sirohydrochlorin cobaltochelatase activity |
A | 0019251 | biological_process | anaerobic cobalamin biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0046906 | molecular_function | tetrapyrrole binding |
A | 0050897 | molecular_function | cobalt ion binding |
B | 0009236 | biological_process | cobalamin biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0016852 | molecular_function | sirohydrochlorin cobaltochelatase activity |
B | 0019251 | biological_process | anaerobic cobalamin biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0046906 | molecular_function | tetrapyrrole binding |
B | 0050897 | molecular_function | cobalt ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 133 |
Chain | Residue |
A | GLY0 |
A | MET1 |
A | MET1 |
A | ARG2 |
A | ASP35 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 B 133 |
Chain | Residue |
A | TYR111 |
B | LEU23 |
B | ARG27 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 B 134 |
Chain | Residue |
A | ARG27 |
B | TYR111 |
A | LEU23 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 B 135 |
Chain | Residue |
A | TYR17 |
B | PHE68 |
B | ILE69 |
B | SER70 |
B | HOH148 |
B | HOH156 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 201 |
Chain | Residue |
A | GLY0 |
A | ARG2 |
A | GOL203 |
A | HOH204 |
B | ASP60 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 202 |
Chain | Residue |
A | ILE69 |
A | SER70 |
B | HOH156 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 203 |
Chain | Residue |
A | GOL201 |
B | MET1 |
B | ARG2 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00785","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21173279","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00785","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16835730","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21173279","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00785","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21173279","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XWQ","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |