2W8R
The crystal structure of human SSADH in complex with NAD+
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 | 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 | 10 |
Details | BINDING SITE FOR RESIDUE ADP A 702 |
Chain | Residue |
A | THR202 |
A | THR288 |
A | TRP204 |
A | LYS228 |
A | ALA230 |
A | GLU231 |
A | ALA264 |
A | GLY268 |
A | PHE282 |
A | SER285 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1001 |
Chain | Residue |
A | LEU368 |
A | ARG369 |
A | VAL370 |
A | HIS413 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
Chain | Residue |
A | GLN349 |
A | ASP450 |
A | THR451 |
A | GLU452 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 1003 |
Chain | Residue |
A | LEU51 |
A | ARG68 |
A | SER83 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 1004 |
Chain | Residue |
A | ARG350 |
A | LYS448 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 A 1005 |
Chain | Residue |
A | HOH2048 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1006 |
Chain | Residue |
A | TYR159 |
A | PHE206 |
A | ARG334 |
A | SER498 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1007 |
Chain | Residue |
A | VAL95 |
A | ARG96 |
A | ARG261 |
A | LYS262 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1008 |
Chain | Residue |
A | VAL65 |
A | LEU70 |
A | GLY84 |
A | LYS417 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 A 1009 |
Chain | Residue |
A | ARG60 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1010 |
Chain | Residue |
A | TYR159 |
A | ARG213 |
A | ARG334 |
A | VAL341 |
A | SER498 |
A | PHE504 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 1101 |
Chain | Residue |
A | THR408 |
A | GLY409 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 1102 |
Chain | Residue |
A | ARG103 |
A | ASN385 |
A | GLU386 |
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 | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007 |
Chain | Residue | Details |
A | GLU306 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10008 |
Chain | Residue | Details |
A | ALA340 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P20000 |
Chain | Residue | Details |
A | GLU306 | |
A | GLU438 | |
A | THR202 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19300440, ECO:0007744|PDB:2W8Q |
Chain | Residue | Details |
A | ARG334 | |
A | SER498 | |
A | ARG213 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19300440, ECO:0007744|PDB:2W8R |
Chain | Residue | Details |
A | LYS228 | |
A | GLY284 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P20000 |
Chain | Residue | Details |
A | ASN205 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q8BWF0 |
Chain | Residue | Details |
A | LYS265 | |
A | LYS126 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8BWF0 |
Chain | Residue | Details |
A | LYS402 | |
A | LYS135 | |
A | LYS184 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8BWF0 |
Chain | Residue | Details |
A | LYS365 | |
A | LYS411 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER499 |