1WTJ
Crystal Structure of delta1-piperideine-2-carboxylate reductase from Pseudomonas syringae pvar.tomato
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0006560 | biological_process | proline metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030416 | biological_process | methylamine metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0047125 | molecular_function | delta1-piperideine-2-carboxylate reductase activity |
| A | 0050132 | molecular_function | N-methylalanine dehydrogenase activity |
| A | 0050241 | molecular_function | pyrroline-2-carboxylate reductase activity |
| A | 0070401 | molecular_function | NADP+ binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0006560 | biological_process | proline metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030416 | biological_process | methylamine metabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0047125 | molecular_function | delta1-piperideine-2-carboxylate reductase activity |
| B | 0050132 | molecular_function | N-methylalanine dehydrogenase activity |
| B | 0050241 | molecular_function | pyrroline-2-carboxylate reductase activity |
| B | 0070401 | molecular_function | NADP+ binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"16192274","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"16192274","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16192274","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"16192274","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2CWF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CWH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16192274","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2CWF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CWH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1s20 |
| Chain | Residue | Details |
| A | HIS54 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1s20 |
| Chain | Residue | Details |
| B | HIS54 |
