1HYO
CRYSTAL STRUCTURE OF FUMARYLACETOACETATE HYDROLASE COMPLEXED WITH 4-(HYDROXYMETHYLPHOSPHINOYL)-3-OXO-BUTANOIC ACID
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 | L-arginine catabolic process |
| A | 0006559 | biological_process | L-phenylalanine catabolic process |
| A | 0006572 | biological_process | L-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 | L-arginine catabolic process |
| B | 0006559 | biological_process | L-phenylalanine catabolic process |
| B | 0006572 | biological_process | L-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 MG A 1004 |
| Chain | Residue |
| A | ASP233 |
| A | TRP234 |
| A | LYS253 |
| A | GLY256 |
| A | THR257 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1005 |
| Chain | Residue |
| B | THR757 |
| B | ASP733 |
| B | TRP734 |
| B | LYS753 |
| B | GLY756 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 1006 |
| Chain | Residue |
| A | ASP126 |
| A | GLU199 |
| A | GLU201 |
| A | ASP233 |
| A | HBU1012 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 1007 |
| Chain | Residue |
| B | ASP626 |
| B | GLU699 |
| B | GLU701 |
| B | ASP733 |
| B | HBU1011 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI B 1008 |
| Chain | Residue |
| A | HIS222 |
| B | GLY499 |
| B | HOH1272 |
| B | HOH1319 |
| B | HOH1320 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 1009 |
| Chain | Residue |
| A | TYR128 |
| A | ARG142 |
| A | HBU1012 |
| A | HOH1073 |
| A | HOH1079 |
| B | PRO746 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 1010 |
| Chain | Residue |
| A | PRO246 |
| B | TYR628 |
| B | ARG642 |
| B | LEU649 |
| B | HOH1043 |
| B | HOH1044 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HBU B 1011 |
| Chain | Residue |
| B | ASP626 |
| B | PHE627 |
| B | TYR628 |
| B | HIS633 |
| B | TYR659 |
| B | GLU699 |
| B | GLU701 |
| B | ARG737 |
| B | GLN740 |
| B | LYS753 |
| B | GLY849 |
| B | THR850 |
| B | CA1007 |
| B | HOH1071 |
| B | HOH1318 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HBU A 1012 |
| Chain | Residue |
| A | ASP126 |
| A | PHE127 |
| A | TYR128 |
| A | HIS133 |
| A | TYR159 |
| A | GLU199 |
| A | GLU201 |
| A | ARG237 |
| A | GLN240 |
| A | LYS253 |
| A | GLY349 |
| A | THR350 |
| A | CA1006 |
| A | ACT1009 |
| A | HOH1114 |
| A | HOH1301 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"10508789","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10508789","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11154690","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10508789","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11154690","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"UniProtKB","id":"P16930","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P16930","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P25093","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 | ARG737 | |
| B | LYS753 | |
| B | GLN740 | |
| B | HIS633 | |
| B | GLU864 |
| 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 | ASP626 | metal ligand |
| B | GLU864 | electrostatic stabiliser, hydrogen bond acceptor |
| B | HIS633 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU699 | hydrogen bond acceptor, metal ligand, steric role |
| B | GLU701 | metal ligand |
| B | ASP733 | metal ligand |
| B | ARG737 | electrostatic stabiliser, hydrogen bond donor |
| B | GLN740 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS753 | metal ligand |
| B | THR757 | metal ligand |
