3TSN
4-hydroxythreonine-4-phosphate dehydrogenase from Campylobacter jejuni
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 | 0016491 | molecular_function | oxidoreductase 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 | 0016491 | molecular_function | oxidoreductase 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 |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0008615 | biological_process | pyridoxine biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050570 | molecular_function | 4-hydroxythreonine-4-phosphate dehydrogenase activity |
| C | 0050897 | molecular_function | cobalt ion binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0008615 | biological_process | pyridoxine biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050570 | molecular_function | 4-hydroxythreonine-4-phosphate dehydrogenase activity |
| D | 0050897 | molecular_function | cobalt ion binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI A 501 |
| Chain | Residue |
| A | HIS177 |
| A | HIS301 |
| B | HIS216 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI B 501 |
| Chain | Residue |
| A | HIS216 |
| B | HIS177 |
| B | HIS301 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI C 501 |
| Chain | Residue |
| C | HIS177 |
| C | HIS301 |
| D | HIS216 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI D 501 |
| Chain | Residue |
| C | HIS216 |
| D | HIS177 |
| D | HIS301 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02086","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02086","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"SEP-2011","submissionDatabase":"PDB data bank","title":"4-hydroxythreonine-4-phosphate dehydrogenase from Campylobacter jejuni.","authors":["Osipiuk J.","Gu M.","Kwon K.","Anderson W.F.","Joachimiak A."]}}]} |
| Chain | Residue | Details |






