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 | ACT_SITE: Charge relay system => ECO:0000305|PubMed:16192274 |
Chain | Residue | Details |
A | SER53 | |
A | ASP194 | |
B | SER53 | |
B | ASP194 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:16192274 |
Chain | Residue | Details |
A | HIS54 | |
B | HIS54 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:16192274 |
Chain | Residue | Details |
A | ARG58 | |
A | THR166 | |
A | HIS192 | |
B | ARG58 | |
B | THR166 | |
B | HIS192 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: in other chain => ECO:0000269|PubMed:16192274, ECO:0007744|PDB:2CWF, ECO:0007744|PDB:2CWH |
Chain | Residue | Details |
A | HIS126 | |
A | ASP184 | |
A | ARG309 | |
B | HIS126 | |
B | ASP184 | |
B | ARG309 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16192274, ECO:0007744|PDB:2CWF, ECO:0007744|PDB:2CWH |
Chain | Residue | Details |
A | HIS236 | |
B | HIS236 |
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 |