2GRA
crystal structure of Human Pyrroline-5-carboxylate Reductase complexed with nadp
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| A | 0006561 | biological_process | obsolete proline biosynthetic process |
| B | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| B | 0006561 | biological_process | obsolete proline biosynthetic process |
| C | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| C | 0006561 | biological_process | obsolete proline biosynthetic process |
| D | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| D | 0006561 | biological_process | obsolete proline biosynthetic process |
| E | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| E | 0006561 | biological_process | obsolete proline biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NAP A 1300 |
| Chain | Residue |
| A | ARG129 |
| A | SER220 |
| A | GLU1301 |
| C | LEU201 |
| C | ARG204 |
| C | GLN208 |
| A | GLU130 |
| A | SER154 |
| A | SER155 |
| A | GLY157 |
| A | PHE158 |
| A | LEU217 |
| A | LEU218 |
| A | HIS219 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GLU A 1301 |
| Chain | Residue |
| A | NAP1300 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAP B 2300 |
| Chain | Residue |
| B | ARG129 |
| B | GLU130 |
| B | SER154 |
| B | SER155 |
| B | VAL156 |
| B | GLY157 |
| B | PHE158 |
| B | ARG200 |
| B | LEU201 |
| B | ARG204 |
| B | GLN208 |
| B | LEU217 |
| B | LEU218 |
| B | HIS219 |
| B | GLU221 |
| B | GLU2301 |
| B | HOH2319 |
| B | HOH2338 |
| B | HOH2345 |
| B | HOH2362 |
| B | HOH2364 |
| B | HOH2395 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GLU B 2301 |
| Chain | Residue |
| B | ARG129 |
| B | NAP2300 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAP C 3300 |
| Chain | Residue |
| A | ARG200 |
| A | LEU201 |
| A | ARG204 |
| A | GLN208 |
| C | ARG129 |
| C | GLU130 |
| C | SER154 |
| C | SER155 |
| C | VAL156 |
| C | GLY157 |
| C | PHE158 |
| C | LEU218 |
| C | SER220 |
| C | GLU3301 |
| C | HOH3320 |
| C | HOH3394 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GLU C 3301 |
| Chain | Residue |
| C | NAP3300 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAP D 4300 |
| Chain | Residue |
| D | GLU130 |
| D | SER154 |
| D | SER155 |
| D | GLY157 |
| D | PHE158 |
| D | LEU217 |
| D | LEU218 |
| D | HIS219 |
| D | SER220 |
| D | GLU221 |
| D | GLU4301 |
| D | HOH4315 |
| E | ARG200 |
| E | LEU201 |
| E | ARG204 |
| E | GLN208 |
| E | HOH5318 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GLU D 4301 |
| Chain | Residue |
| D | NAP4300 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAP E 5300 |
| Chain | Residue |
| D | ARG200 |
| D | LEU201 |
| D | ARG204 |
| D | GLN208 |
| E | ARG129 |
| E | GLU130 |
| E | SER154 |
| E | GLY157 |
| E | PHE158 |
| E | LEU217 |
| E | LEU218 |
| E | HIS219 |
| E | GLU221 |
| E | GLU5301 |
| E | HOH5448 |
| E | HOH5451 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GLU E 5301 |
| Chain | Residue |
| E | NAP5300 |
Functional Information from PROSITE/UniProt
| site_id | PS00521 |
| Number of Residues | 23 |
| Details | P5CR Delta 1-pyrroline-5-carboxylate reductase signature. Pgq.LkdnVSSpGGaTihALhvLE |
| Chain | Residue | Details |
| A | PRO224-GLU246 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 50 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human pyrroline-5-carboxylate reductase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28258219","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5UAT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5UAV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28258219","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5UAT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28258219","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5UAV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28258219","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5UAU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 5 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Zebisch A.","Kolch W."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
