2W8O
The crystal structure of the reduced form of human SSADH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004777 | molecular_function | succinate-semialdehyde dehydrogenase (NAD+) activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006105 | biological_process | succinate metabolic process |
| A | 0006536 | biological_process | glutamate metabolic process |
| A | 0007417 | biological_process | central nervous system development |
| A | 0009013 | molecular_function | succinate-semialdehyde dehydrogenase [NAD(P)+] activity |
| A | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| 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 | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 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 701 |
| Chain | Residue |
| A | LEU368 |
| A | VAL370 |
| A | HIS413 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 702 |
| Chain | Residue |
| A | GLN349 |
| A | ASP450 |
| A | THR451 |
| A | GLU452 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 703 |
| Chain | Residue |
| A | SER285 |
| A | THR288 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 704 |
| Chain | Residue |
| A | LEU51 |
| A | ARG68 |
| A | SER83 |
| A | ALA85 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 705 |
| Chain | Residue |
| A | ARG350 |
| A | LYS448 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 706 |
| Chain | Residue |
| A | TYR175 |
| A | LYS518 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 707 |
| Chain | Residue |
| A | TYR159 |
| A | PHE206 |
| A | ARG334 |
| A | SER498 |
| A | SO4708 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 708 |
| Chain | Residue |
| A | TYR159 |
| A | ARG213 |
| A | ARG334 |
| A | VAL341 |
| A | SER498 |
| A | PHE504 |
| A | SO4707 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 801 |
| Chain | Residue |
| A | GLY409 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 802 |
| Chain | Residue |
| A | ARG96 |
| A | ALA100 |
| A | ARG103 |
| A | ASN418 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FrNTGQTCVCSN |
| Chain | Residue | Details |
| A | PHE333-ASN344 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGLAP |
| Chain | Residue | Details |
| A | MET305-PRO312 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P20000","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19300440","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2W8Q","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19300440","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2W8R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P20000","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8BWF0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8BWF0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BWF0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| A | CYS340 | |
| A | GLU306 | |
| A | ASN205 |
