3V9H
Crystal structure of human 1-pyrroline-5-carboxylate dehydrogenase mutant S352A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006560 | biological_process | proline metabolic process |
| A | 0006562 | biological_process | L-proline catabolic process |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0010133 | biological_process | L-proline catabolic process to L-glutamate |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0019470 | biological_process | trans-4-hydroxy-L-proline catabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006560 | biological_process | proline metabolic process |
| B | 0006562 | biological_process | L-proline catabolic process |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0010133 | biological_process | L-proline catabolic process to L-glutamate |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0019470 | biological_process | trans-4-hydroxy-L-proline catabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| C | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0006560 | biological_process | proline metabolic process |
| C | 0006562 | biological_process | L-proline catabolic process |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0010133 | biological_process | L-proline catabolic process to L-glutamate |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0019470 | biological_process | trans-4-hydroxy-L-proline catabolic process |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| D | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0006560 | biological_process | proline metabolic process |
| D | 0006562 | biological_process | L-proline catabolic process |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0010133 | biological_process | L-proline catabolic process to L-glutamate |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0019470 | biological_process | trans-4-hydroxy-L-proline catabolic process |
| D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 564 |
| Chain | Residue |
| A | LYS233 |
| A | SER235 |
| A | ASP236 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 565 |
| Chain | Residue |
| A | SER349 |
| A | GLY512 |
| A | SER513 |
| A | PHE520 |
| A | HOH580 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 564 |
| Chain | Residue |
| B | GLY512 |
| B | SER513 |
| B | PHE520 |
| B | SER349 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 564 |
| Chain | Residue |
| C | SER349 |
| C | THR511 |
| C | GLY512 |
| C | SER513 |
| C | PHE520 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 564 |
| Chain | Residue |
| D | GLU165 |
| D | SER349 |
| D | THR511 |
| D | GLY512 |
| D | SER513 |
| D | PHE520 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 565 |
| Chain | Residue |
| B | ARG47 |
| B | GLN51 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 C 565 |
| Chain | Residue |
| C | ARG47 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FeYGGQKCSACA |
| Chain | Residue | Details |
| A | PHE341-ALA352 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GECGGKNF |
| Chain | Residue | Details |
| A | GLY313-PHE320 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22516612","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8CHT0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 28 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8CHT0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 24 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8CHT0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
