1JXZ
Structure of the H90Q mutant of 4-Chlorobenzoyl-Coenzyme A Dehalogenase complexed with 4-hydroxybenzoyl-Coenzyme A (product)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0015936 | biological_process | coenzyme A metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0018787 | molecular_function | 4-chlorobenzoyl-CoA dehalogenase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0015936 | biological_process | coenzyme A metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0018787 | molecular_function | 4-chlorobenzoyl-CoA dehalogenase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0015936 | biological_process | coenzyme A metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0018787 | molecular_function | 4-chlorobenzoyl-CoA dehalogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 270 |
| Chain | Residue |
| A | GLY49 |
| A | LEU202 |
| A | ALA203 |
| A | ALA205 |
| A | THR207 |
| A | GLN210 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 270 |
| Chain | Residue |
| B | ALA205 |
| B | THR207 |
| B | GLN210 |
| B | GLY49 |
| B | LEU202 |
| B | ALA203 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 270 |
| Chain | Residue |
| C | GLY49 |
| C | LEU202 |
| C | ALA203 |
| C | ALA205 |
| C | THR207 |
| C | GLN210 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 271 |
| Chain | Residue |
| B | GLU57 |
| B | ASP58 |
| B | ASN108 |
| B | ALA128 |
| B | LYS188 |
| B | ARG192 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE BCA A 271 |
| Chain | Residue |
| A | ARG22 |
| A | HIS23 |
| A | ARG24 |
| A | ALA26 |
| A | ALA62 |
| A | GLY63 |
| A | PHE64 |
| A | TYR65 |
| A | LEU66 |
| A | ARG67 |
| A | TRP89 |
| A | GLY113 |
| A | GLY114 |
| A | TRP137 |
| A | ASP145 |
| A | THR146 |
| A | ARG251 |
| A | ASP254 |
| A | HOH338 |
| A | HOH368 |
| A | HOH420 |
| A | HOH460 |
| A | HOH544 |
| A | HOH595 |
| B | PHE252 |
| B | ARG257 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE BCA B 272 |
| Chain | Residue |
| B | ARG22 |
| B | HIS23 |
| B | ARG24 |
| B | ALA62 |
| B | PHE64 |
| B | TYR65 |
| B | LEU66 |
| B | ARG67 |
| B | TRP89 |
| B | GLY113 |
| B | GLY114 |
| B | TRP137 |
| B | ASP145 |
| B | THR146 |
| B | HOH411 |
| B | HOH468 |
| C | LYS19 |
| C | GLU57 |
| C | PHE252 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE BCA C 271 |
| Chain | Residue |
| A | PHE252 |
| A | ARG257 |
| A | ALA258 |
| C | ARG22 |
| C | HIS23 |
| C | ARG24 |
| C | ALA26 |
| C | ALA62 |
| C | GLY63 |
| C | PHE64 |
| C | TYR65 |
| C | LEU66 |
| C | ARG67 |
| C | ALA86 |
| C | TRP89 |
| C | GLY113 |
| C | GLY114 |
| C | TRP137 |
| C | ILE140 |
| C | ASP145 |
| C | THR146 |
| C | HOH299 |
| C | HOH364 |
| C | HOH396 |
| C | HOH436 |
| C | HOH451 |
Functional Information from PROSITE/UniProt
| site_id | PS00166 |
| Number of Residues | 21 |
| Details | ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. LAaINGvaaGGGlgisLaSDM |
| Chain | Residue | Details |
| A | LEU104-MET124 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:8679561, ECO:0000269|PubMed:8718880 |
| Chain | Residue | Details |
| A | GLN90 | |
| B | GLN90 | |
| C | GLN90 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:8679561, ECO:0000269|PubMed:8718880 |
| Chain | Residue | Details |
| A | ASP145 | |
| B | ASP145 | |
| C | ASP145 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:8679561 |
| Chain | Residue | Details |
| A | ARG24 | |
| B | ARG24 | |
| C | ARG24 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: in other chain |
| Chain | Residue | Details |
| A | ALA62 | |
| A | GLY114 | |
| B | ALA62 | |
| B | GLY114 | |
| C | ALA62 | |
| C | GLY114 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ARG257 | |
| B | ARG257 | |
| C | ARG257 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1nzy |
| Chain | Residue | Details |
| A | GLN90 | |
| A | PHE64 | |
| A | ASP145 | |
| A | GLY114 | |
| A | TRP137 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1nzy |
| Chain | Residue | Details |
| B | GLN90 | |
| B | PHE64 | |
| B | ASP145 | |
| B | GLY114 | |
| B | TRP137 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1nzy |
| Chain | Residue | Details |
| C | GLN90 | |
| C | PHE64 | |
| C | ASP145 | |
| C | GLY114 | |
| C | TRP137 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nzy |
| Chain | Residue | Details |
| A | ASP145 | |
| A | TRP137 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nzy |
| Chain | Residue | Details |
| B | ASP145 | |
| B | TRP137 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nzy |
| Chain | Residue | Details |
| C | ASP145 | |
| C | TRP137 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 24 |
| Chain | Residue | Details |
| A | PHE64 | electrostatic stabiliser, hydrogen bond donor |
| A | ALA86 | activator, hydrogen bond acceptor |
| A | GLN90 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLY114 | electrostatic stabiliser, hydrogen bond donor |
| A | TRP137 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP145 | covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 24 |
| Chain | Residue | Details |
| B | PHE64 | electrostatic stabiliser, hydrogen bond donor |
| B | ALA86 | activator, hydrogen bond acceptor |
| B | GLN90 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLY114 | electrostatic stabiliser, hydrogen bond donor |
| B | TRP137 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP145 | covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 24 |
| Chain | Residue | Details |
| C | PHE64 | electrostatic stabiliser, hydrogen bond donor |
| C | ALA86 | activator, hydrogen bond acceptor |
| C | GLN90 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | GLY114 | electrostatic stabiliser, hydrogen bond donor |
| C | TRP137 | electrostatic stabiliser, hydrogen bond donor |
| C | ASP145 | covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor |
