1PS6
Crystal structure of E.coli PdxA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008615 | biological_process | pyridoxine biosynthetic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050570 | molecular_function | 4-hydroxythreonine-4-phosphate dehydrogenase activity |
| A | 0050897 | molecular_function | cobalt ion binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008615 | biological_process | pyridoxine biosynthetic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050570 | molecular_function | 4-hydroxythreonine-4-phosphate dehydrogenase activity |
| B | 0050897 | molecular_function | cobalt ion binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 330 |
| Chain | Residue |
| A | HIS166 |
| A | HIS266 |
| A | 4TP332 |
| B | HIS211 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 331 |
| Chain | Residue |
| A | HIS211 |
| B | HIS166 |
| B | HIS266 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 4TP A 332 |
| Chain | Residue |
| A | LEU153 |
| A | HIS166 |
| A | HIS266 |
| A | LEU270 |
| A | LYS274 |
| A | ASN283 |
| A | ARG292 |
| A | ZN330 |
| B | HIS211 |
| A | HIS136 |
| A | THR137 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00536","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12896974","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00536","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12896974","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
