2HZY
Mouse fumarylacetoacetate hydrolase complexes with a transition-state mimic of the complete substrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004334 | molecular_function | fumarylacetoacetase activity |
| A | 0006527 | biological_process | arginine catabolic process |
| A | 0006559 | biological_process | L-phenylalanine catabolic process |
| A | 0006572 | biological_process | tyrosine catabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0009072 | biological_process | aromatic amino acid metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004334 | molecular_function | fumarylacetoacetase activity |
| B | 0006527 | biological_process | arginine catabolic process |
| B | 0006559 | biological_process | L-phenylalanine catabolic process |
| B | 0006572 | biological_process | tyrosine catabolic process |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0009072 | biological_process | aromatic amino acid metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1201 |
| Chain | Residue |
| A | ASP233 |
| A | TRP234 |
| A | LYS253 |
| A | GLY256 |
| A | THR257 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 1202 |
| Chain | Residue |
| B | THR257 |
| B | ASP233 |
| B | TRP234 |
| B | LYS253 |
| B | GLY256 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 1203 |
| Chain | Residue |
| A | ASP126 |
| A | GLU199 |
| A | GLU201 |
| A | ASP233 |
| A | DHJ1102 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 1204 |
| Chain | Residue |
| B | ASP126 |
| B | GLU199 |
| B | GLU201 |
| B | ASP233 |
| B | DHJ1101 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI B 1205 |
| Chain | Residue |
| A | HIS222 |
| A | HOH1477 |
| B | GLY-1 |
| B | HOH1447 |
| B | HOH1448 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1206 |
| Chain | Residue |
| A | GLY122 |
| A | ASP123 |
| A | HOH1343 |
| B | GLY122 |
| B | ASP123 |
| B | HOH1274 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI B 1207 |
| Chain | Residue |
| B | HIS154 |
| B | HOH1221 |
| B | HOH1506 |
| B | HOH1520 |
| B | HOH1537 |
| B | HOH1677 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI B 1208 |
| Chain | Residue |
| B | ASP11 |
| B | HIS395 |
| B | HOH1454 |
| B | HOH1468 |
| B | HOH1703 |
| B | HOH1714 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI A 1209 |
| Chain | Residue |
| A | ASP11 |
| A | HIS395 |
| A | HOH1285 |
| A | HOH1292 |
| A | HOH1518 |
| A | HOH1534 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI B 1210 |
| Chain | Residue |
| B | ASP296 |
| B | HOH1282 |
| B | HOH1642 |
| B | HOH1676 |
| B | HOH1709 |
| B | HOH1723 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI A 1211 |
| Chain | Residue |
| A | HIS154 |
| A | HOH1290 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI A 1212 |
| Chain | Residue |
| A | ASP399 |
| A | HOH1597 |
| A | HOH1668 |
| A | HOH1669 |
| A | HOH1670 |
| B | HIS222 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI A 1213 |
| Chain | Residue |
| A | HIS48 |
| A | HOH1423 |
| A | HOH1591 |
| A | HOH1634 |
| A | HOH1671 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI A 1214 |
| Chain | Residue |
| A | HIS58 |
| A | HOH1646 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI B 1215 |
| Chain | Residue |
| B | HIS58 |
| B | HOH1499 |
| site_id | BC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE DHJ B 1101 |
| Chain | Residue |
| A | PRO246 |
| A | LEU247 |
| B | ASP126 |
| B | PHE127 |
| B | TYR128 |
| B | HIS133 |
| B | VAL137 |
| B | PHE141 |
| B | ARG142 |
| B | TYR159 |
| B | GLU199 |
| B | GLU201 |
| B | ASP233 |
| B | ARG237 |
| B | GLN240 |
| B | LYS253 |
| B | GLY349 |
| B | THR350 |
| B | MN1204 |
| B | HOH1252 |
| B | HOH1254 |
| site_id | BC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE DHJ A 1102 |
| Chain | Residue |
| A | TYR159 |
| A | GLU199 |
| A | GLU201 |
| A | ASP233 |
| A | ARG237 |
| A | GLN240 |
| A | LYS253 |
| A | GLY349 |
| A | THR350 |
| A | MN1203 |
| A | HOH1259 |
| A | HOH1503 |
| B | PRO246 |
| A | ASP126 |
| A | PHE127 |
| A | TYR128 |
| A | HIS133 |
| A | VAL137 |
| A | ARG142 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:10508789 |
| Chain | Residue | Details |
| A | HIS133 | |
| B | HIS133 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 |
| Chain | Residue | Details |
| A | ASP126 | |
| A | GLU199 | |
| A | GLU201 | |
| B | ASP126 | |
| B | GLU199 | |
| B | GLU201 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:10508789 |
| Chain | Residue | Details |
| A | TYR128 | |
| B | THR350 | |
| A | ARG142 | |
| A | GLN240 | |
| A | TYR244 | |
| A | THR350 | |
| B | TYR128 | |
| B | ARG142 | |
| B | GLN240 | |
| B | TYR244 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11154690 |
| Chain | Residue | Details |
| A | ASP233 | |
| A | LYS253 | |
| A | THR257 | |
| B | ASP233 | |
| B | LYS253 | |
| B | THR257 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P16930 |
| Chain | Residue | Details |
| A | SER2 | |
| B | SER2 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| A | SER84 | |
| A | SER92 | |
| B | SER84 | |
| B | SER92 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P16930 |
| Chain | Residue | Details |
| A | SER309 | |
| B | SER309 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P25093 |
| Chain | Residue | Details |
| A | SER417 | |
| B | SER417 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1qcn |
| Chain | Residue | Details |
| A | HIS133 | |
| A | GLU364 | |
| A | ARG237 | |
| A | GLN240 | |
| A | LYS253 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1qcn |
| Chain | Residue | Details |
| B | HIS133 | |
| B | GLU364 | |
| B | ARG237 | |
| B | GLN240 | |
| B | LYS253 |
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 180 |
| Chain | Residue | Details |
| A | ASP126 | metal ligand |
| A | GLU364 | electrostatic stabiliser, hydrogen bond acceptor |
| A | HIS133 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU199 | hydrogen bond acceptor, metal ligand, steric role |
| A | GLU201 | metal ligand |
| A | ASP233 | metal ligand |
| A | ARG237 | electrostatic stabiliser, hydrogen bond donor |
| A | GLN240 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS253 | metal ligand |
| A | THR257 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 180 |
| Chain | Residue | Details |
| B | ASP126 | metal ligand |
| B | GLU364 | electrostatic stabiliser, hydrogen bond acceptor |
| B | HIS133 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU199 | hydrogen bond acceptor, metal ligand, steric role |
| B | GLU201 | metal ligand |
| B | ASP233 | metal ligand |
| B | ARG237 | electrostatic stabiliser, hydrogen bond donor |
| B | GLN240 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS253 | metal ligand |
| B | THR257 | metal ligand |
