1QQJ
CRYSTAL STRUCTURE OF MOUSE FUMARYLACETOACETATE HYDROLASE REFINED AT 1.55 ANGSTROM RESOLUTION
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 |
| A | 1902000 | biological_process | homogentisate catabolic process |
| 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 |
| B | 1902000 | biological_process | homogentisate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 420 |
| Chain | Residue |
| B | ASP126 |
| B | GLU199 |
| B | GLU201 |
| B | ASP233 |
| B | HOH2090 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 420 |
| Chain | Residue |
| A | LYS253 |
| A | HOH2068 |
| A | HOH2072 |
| A | ASP126 |
| A | GLU199 |
| A | GLU201 |
| A | ASP233 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 2000 |
| Chain | Residue |
| A | PRO246 |
| B | TYR128 |
| B | VAL137 |
| B | ARG142 |
| B | HOH2054 |
| B | HOH2061 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 2001 |
| Chain | Residue |
| A | TYR128 |
| A | VAL137 |
| A | ARG142 |
| A | CAC2004 |
| A | HOH2032 |
| A | HOH2033 |
| B | PRO246 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CAC B 2003 |
| Chain | Residue |
| B | TYR128 |
| B | HIS133 |
| B | GLU199 |
| B | ARG237 |
| B | GLN240 |
| B | LYS253 |
| B | HOH2090 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CAC A 2004 |
| Chain | Residue |
| A | TYR128 |
| A | HIS133 |
| A | VAL137 |
| A | GLU199 |
| A | ARG237 |
| A | GLN240 |
| A | LYS253 |
| A | THR350 |
| A | ACT2001 |
| A | HOH2068 |
| A | HOH2072 |
| B | LEU247 |
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 |
| B | ARG142 | |
| B | GLN240 | |
| B | TYR244 | |
| B | THR350 | |
| A | TYR128 | |
| A | ARG142 | |
| A | GLN240 | |
| A | TYR244 | |
| A | THR350 | |
| B | TYR128 |
| 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 | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 180 |
| Chain | Residue | Details |
| A | ASP126 | metal ligand |
| 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 | THR257 | metal ligand |
| A | GLU364 | electrostatic stabiliser, hydrogen bond acceptor |
| A | LYS253 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 180 |
| Chain | Residue | Details |
| B | ASP126 | metal ligand |
| 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 | THR257 | metal ligand |
| B | GLU364 | electrostatic stabiliser, hydrogen bond acceptor |
| B | LYS253 | metal ligand |
