2W8Q
The crystal structure of human SSADH in complex with SSA.
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 | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| A | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| A | 0009791 | biological_process | post-embryonic development |
| 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 |
| A | 0045202 | cellular_component | synapse |
| A | 0051932 | biological_process | synaptic transmission, GABAergic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1001 |
| Chain | Residue |
| A | LEU368 |
| A | ARG369 |
| A | VAL370 |
| A | HIS413 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
| Chain | Residue |
| A | GLN349 |
| A | THR451 |
| A | GLU452 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1003 |
| Chain | Residue |
| A | THR288 |
| A | PHE282 |
| A | SER285 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1004 |
| Chain | Residue |
| A | ARG68 |
| A | SER83 |
| A | ALA85 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1005 |
| Chain | Residue |
| A | ARG350 |
| A | LYS448 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1006 |
| Chain | Residue |
| A | TYR175 |
| A | HOH2066 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1007 |
| Chain | Residue |
| A | GLY155 |
| A | GLU156 |
| A | TYR159 |
| A | ARG334 |
| A | SIN3001 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1008 |
| Chain | Residue |
| A | VAL95 |
| A | ARG96 |
| A | ARG261 |
| A | LYS262 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1009 |
| Chain | Residue |
| A | ARG68 |
| A | TRP69 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 1101 |
| Chain | Residue |
| A | THR408 |
| A | GLY409 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1102 |
| Chain | Residue |
| A | ARG103 |
| A | ASN385 |
| A | GLU386 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SIN A 3001 |
| Chain | Residue |
| A | TYR159 |
| A | PHE206 |
| A | ARG213 |
| A | GLU306 |
| A | ARG334 |
| A | ALA340 |
| A | SER498 |
| A | SO41007 |
Functional Information from PROSITE/UniProt
| 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 | 5 |
| 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 |
