2CWH
Crystal Structure of delta1-piperideine-2-carboxylate reductase from Pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate
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 | 34 |
| Details | BINDING SITE FOR RESIDUE NDP A 2510 |
| Chain | Residue |
| A | HIS54 |
| A | PHE183 |
| A | ASP184 |
| A | LEU185 |
| A | ALA186 |
| A | ARG309 |
| A | GLY312 |
| A | ARG314 |
| A | ARG315 |
| A | PYC2520 |
| A | HOH2536 |
| A | HIS126 |
| A | HOH2545 |
| A | HOH2571 |
| A | HOH2576 |
| A | HOH2581 |
| A | HOH2634 |
| A | HOH2645 |
| A | HOH2709 |
| A | HOH2724 |
| A | HOH2728 |
| A | HOH2750 |
| A | ALA128 |
| B | HIS157 |
| B | HIS236 |
| B | LYS237 |
| B | HOH1539 |
| B | HOH1640 |
| A | ALA129 |
| A | LEU130 |
| A | VAL148 |
| A | SER150 |
| A | THR166 |
| A | PRO168 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NDP B 1510 |
| Chain | Residue |
| A | HIS236 |
| A | LYS237 |
| A | HOH2533 |
| A | HOH2560 |
| A | HOH2697 |
| B | HIS54 |
| B | HIS126 |
| B | ALA128 |
| B | ALA129 |
| B | LEU130 |
| B | VAL148 |
| B | SER150 |
| B | THR166 |
| B | PRO168 |
| B | PHE183 |
| B | ASP184 |
| B | LEU185 |
| B | ALA186 |
| B | ARG309 |
| B | GLY312 |
| B | ASP313 |
| B | ARG314 |
| B | ARG315 |
| B | PYC1520 |
| B | HOH1533 |
| B | HOH1580 |
| B | HOH1599 |
| B | HOH1611 |
| B | HOH1685 |
| B | HOH1741 |
| B | HOH1777 |
| B | HOH1779 |
| B | HOH1787 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PYC A 2520 |
| Chain | Residue |
| A | HIS54 |
| A | ARG58 |
| A | MET151 |
| A | THR166 |
| A | ALA191 |
| A | HIS192 |
| A | GLY193 |
| A | NDP2510 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYC B 1520 |
| Chain | Residue |
| B | HIS54 |
| B | ARG58 |
| B | SER150 |
| B | MET151 |
| B | THR166 |
| B | ALA191 |
| B | HIS192 |
| B | GLY193 |
| B | NDP1510 |
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 |
