1NZY
4-CHLOROBENZOYL COENZYME A DEHALOGENASE FROM PSEUDOMONAS SP. STRAIN CBS-3
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 271 |
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 271 |
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 271 |
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 902 |
Chain | Residue |
B | GLU57 |
B | ASP58 |
B | ASN108 |
B | ALA128 |
B | LYS188 |
B | ARG192 |
site_id | AC5 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE BCA A 272 |
Chain | Residue |
A | ARG22 |
A | HIS23 |
A | ARG24 |
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 | HIS256 |
A | HOH313 |
A | HOH354 |
A | HOH429 |
A | HOH432 |
A | HOH462 |
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 | GLY63 |
B | PHE64 |
B | TYR65 |
B | LEU66 |
B | ARG67 |
B | TRP89 |
B | GLY113 |
B | GLY114 |
B | TRP137 |
B | ASP145 |
B | THR146 |
C | LYS19 |
C | GLU57 |
C | PHE252 |
C | ALA258 |
site_id | AC7 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE BCA C 272 |
Chain | Residue |
A | PHE252 |
A | ARG257 |
A | ALA258 |
A | ASP259 |
C | ARG22 |
C | HIS23 |
C | ARG24 |
C | ALA26 |
C | ALA62 |
C | GLY63 |
C | PHE64 |
C | TYR65 |
C | LEU66 |
C | ARG67 |
C | TRP89 |
C | GLY113 |
C | GLY114 |
C | TRP137 |
C | ILE140 |
C | ASP145 |
C | THR146 |
C | HOH330 |
C | HOH345 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 900 |
Chain | Residue |
A | GLU201 |
A | PRO261 |
A | GLN262 |
A | GLU264 |
A | HOH318 |
A | HOH424 |
B | ARG251 |
B | HIS256 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 901 |
Chain | Residue |
B | TYR2 |
B | GLU3 |
B | ILE5 |
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 | |
B | LEU104-MET124 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:8679561, ECO:0000269|PubMed:8718880 |
Chain | Residue | Details |
B | HIS90 | |
C | HIS90 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:8679561, ECO:0000269|PubMed:8718880 |
Chain | Residue | Details |
B | ASP145 | |
C | ASP145 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: in other chain => ECO:0000269|PubMed:8679561 |
Chain | Residue | Details |
B | ARG24 | |
C | ARG24 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: in other chain |
Chain | Residue | Details |
B | ALA62 | |
B | GLY114 | |
C | ALA62 | |
C | GLY114 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: |
Chain | Residue | Details |
B | ARG257 | |
C | ARG257 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | a catalytic site defined by CSA, PubMed 8679561, 8718880, 9254617, Zheng1997 |
Chain | Residue | Details |
A | HIS90 | |
A | PHE64 | |
A | ASP145 | |
A | GLY114 | |
A | TRP137 |
site_id | CSA2 |
Number of Residues | 5 |
Details | a catalytic site defined by CSA, PubMed 8679561, 8718880, 9254617, Zheng1997 |
Chain | Residue | Details |
C | HIS90 | |
C | PHE64 | |
C | ASP145 | |
C | GLY114 | |
C | TRP137 |
site_id | CSA3 |
Number of Residues | 5 |
Details | a catalytic site defined by CSA, PubMed 8679561, 8718880, 9254617, Zheng1997 |
Chain | Residue | Details |
B | HIS90 | |
B | PHE64 | |
B | ASP145 | |
B | GLY114 | |
B | TRP137 |
site_id | MCSA1 |
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 | HIS90 | 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 | MCSA2 |
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 | HIS90 | 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 |