2CWF
Crystal Structure of delta1-piperideine-2-carboxylate reductase from Pseudomonas syringae complexed with NADPH
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 PDB Data
site_id | AC1 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NDP A 2510 |
Chain | Residue |
A | HIS54 |
A | ASP184 |
A | LEU185 |
A | ALA186 |
A | ARG309 |
A | PRO311 |
A | GLY312 |
A | ARG314 |
A | ARG315 |
A | HOH2552 |
A | HOH2564 |
A | HIS126 |
A | HOH2611 |
A | HOH2657 |
A | HOH2697 |
A | HOH2731 |
A | HOH2758 |
A | HOH2767 |
A | HOH2772 |
B | HIS236 |
B | LYS237 |
B | HOH1607 |
A | ALA128 |
A | ALA129 |
A | LEU130 |
A | SER150 |
A | THR166 |
A | PRO168 |
A | PHE183 |
site_id | AC2 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE NDP B 1510 |
Chain | Residue |
A | HIS157 |
A | HIS236 |
A | LYS237 |
A | HOH2519 |
A | HOH2572 |
B | HIS54 |
B | HIS126 |
B | ALA128 |
B | ALA129 |
B | LEU130 |
B | SER150 |
B | THR166 |
B | PRO168 |
B | PHE183 |
B | ASP184 |
B | LEU185 |
B | ALA186 |
B | ALA191 |
B | ARG309 |
B | GLY312 |
B | ASP313 |
B | ARG314 |
B | ARG315 |
B | HOH1543 |
B | HOH1593 |
B | HOH1615 |
B | HOH1640 |
B | HOH1651 |
B | HOH1652 |
B | HOH1683 |
B | HOH1703 |
B | HOH1753 |
B | HOH1754 |
B | HOH1756 |
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 |