2XWQ
Anaerobic cobalt chelatase from Archeaoglobus fulgidus (CbiX) in complex with metalated sirohydrochlorin product
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 |
C | 0009236 | biological_process | cobalamin biosynthetic process |
C | 0016829 | molecular_function | lyase activity |
C | 0016852 | molecular_function | sirohydrochlorin cobaltochelatase activity |
C | 0019251 | biological_process | anaerobic cobalamin biosynthetic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0046906 | molecular_function | tetrapyrrole binding |
C | 0050897 | molecular_function | cobalt ion binding |
D | 0009236 | biological_process | cobalamin biosynthetic process |
D | 0016829 | molecular_function | lyase activity |
D | 0016852 | molecular_function | sirohydrochlorin cobaltochelatase activity |
D | 0019251 | biological_process | anaerobic cobalamin biosynthetic process |
D | 0046872 | molecular_function | metal ion binding |
D | 0046906 | molecular_function | tetrapyrrole binding |
D | 0050897 | molecular_function | cobalt ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE SIR B 1126 |
Chain | Residue |
A | HIS10 |
A | GLY72 |
A | LEU73 |
A | HIS74 |
A | HOH2005 |
A | HOH2025 |
B | HIS10 |
B | GLY11 |
B | SER12 |
B | ARG44 |
B | ARG46 |
A | GLY11 |
B | PHE68 |
B | ILE69 |
B | SER70 |
B | GLY72 |
B | LEU73 |
B | HIS74 |
B | HOH2056 |
B | HOH2057 |
B | HOH2058 |
B | HOH2059 |
A | SER12 |
A | GLN13 |
A | ARG44 |
A | ARG46 |
A | PHE68 |
A | ILE69 |
A | SER70 |
site_id | AC2 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE SIR D 1126 |
Chain | Residue |
C | HIS10 |
C | SER12 |
C | GLN13 |
C | TYR17 |
C | ARG44 |
C | ARG46 |
C | ARG47 |
C | ARG55 |
C | PHE68 |
C | ILE69 |
C | SER70 |
C | GLY72 |
C | LEU73 |
C | HIS74 |
D | HIS10 |
D | SER12 |
D | TYR17 |
D | ARG44 |
D | ARG46 |
D | PHE68 |
D | ILE69 |
D | SER70 |
D | GLY72 |
D | LEU73 |
D | HIS74 |
D | HOH2047 |
D | HOH2048 |
D | HOH2049 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
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 | 8 |
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 | 24 |
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 |