4K4D
X-ray crystal structure of E. coli YbdB complexed with 2,4-dihydroxyphenacyl-CoA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0009239 | biological_process | enterobactin biosynthetic process |
A | 0016289 | molecular_function | acyl-CoA hydrolase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
A | 0016790 | molecular_function | thiolester hydrolase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0009239 | biological_process | enterobactin biosynthetic process |
B | 0016289 | molecular_function | acyl-CoA hydrolase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
B | 0016790 | molecular_function | thiolester hydrolase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HFQ A 201 |
Chain | Residue |
A | GLN48 |
B | THR64 |
B | SER67 |
B | MET68 |
B | VAL81 |
B | GLY82 |
B | THR83 |
B | HIS106 |
B | GLY108 |
B | ARG109 |
B | GLN110 |
A | LEU53 |
B | ASN111 |
B | LEU136 |
B | ACT203 |
A | HIS54 |
A | GLY55 |
A | ASP76 |
A | HIS89 |
A | HIS90 |
A | ARG91 |
A | PRO92 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MLI A 202 |
Chain | Residue |
A | ASP10 |
A | HOH321 |
A | HOH328 |
B | GLY123 |
B | ARG124 |
B | ARG125 |
site_id | AC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HFQ B 201 |
Chain | Residue |
A | THR64 |
A | SER67 |
A | VAL81 |
A | GLY82 |
A | GLY108 |
A | ARG109 |
A | GLN110 |
A | ASN111 |
A | LEU136 |
B | GLN48 |
B | PRO49 |
B | LEU53 |
B | HIS54 |
B | GLY55 |
B | ARG75 |
B | GLY77 |
B | HIS89 |
B | HIS90 |
B | ARG91 |
B | PRO92 |
B | ACT202 |
B | HOH312 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT B 202 |
Chain | Residue |
A | PHE71 |
B | PRO49 |
B | PHE50 |
B | HFQ201 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 203 |
Chain | Residue |
A | PRO49 |
A | HFQ201 |
B | THR15 |
B | MET68 |
B | PHE71 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile or proton acceptor => ECO:0000255|HAMAP-Rule:MF_00907, ECO:0000303|PubMed:25010423, ECO:0000305|PubMed:19193103 |
Chain | Residue | Details |
A | GLU63 | |
B | GLU63 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25010423 |
Chain | Residue | Details |
A | GLN48 | |
A | HIS54 | |
A | GLY82 | |
A | HIS89 | |
B | GLN48 | |
B | HIS54 | |
B | GLY82 | |
B | HIS89 |