3BPT
Crystal structure of human beta-hydroxyisobutyryl-CoA hydrolase in complex with quercetin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003860 | molecular_function | 3-hydroxyisobutyryl-CoA hydrolase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006574 | biological_process | valine catabolic process |
| A | 0009083 | biological_process | branched-chain amino acid catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE QUE A 501 |
| Chain | Residue |
| A | PHE56 |
| A | LEU350 |
| A | HIU502 |
| A | HOH886 |
| A | HOH924 |
| A | LEU57 |
| A | ALA59 |
| A | GLY97 |
| A | GLY98 |
| A | ILE100 |
| A | PRO168 |
| A | ILE172 |
| A | VAL349 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HIU A 502 |
| Chain | Residue |
| A | GLY97 |
| A | GLY98 |
| A | ILE100 |
| A | PHE118 |
| A | GLU121 |
| A | GLY146 |
| A | GLU169 |
| A | LEU174 |
| A | ASP177 |
| A | VAL178 |
| A | QUE501 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU121 | |
| A | GLY146 | |
| A | GLU169 | |
| A | ASP177 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q8QZS1 |
| Chain | Residue | Details |
| A | LYS55 | |
| A | LYS92 | |
| A | LYS221 | |
| A | LYS297 | |
| A | LYS353 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER234 | |
| A | SER356 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8QZS1 |
| Chain | Residue | Details |
| A | LYS257 | |
| A | LYS301 | |
| A | LYS377 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8QZS1 |
| Chain | Residue | Details |
| A | LYS360 | |
| A | LYS365 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| A | ASP177 | |
| A | GLU169 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| A | GLU169 | |
| A | GLY149 | |
| A | GLY146 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 345 |
| Chain | Residue | Details |
| A | GLY98 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY146 | electrostatic stabiliser, hydrogen bond donor |
| A | GLU169 | activator, covalently attached, electrofuge, electrophile, hydrogen bond donor, nucleophile, polar interaction, proton donor |
| A | ASP177 | hydrogen bond acceptor, hydrogen bond donor, increase acidity, proton acceptor, proton donor |
