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 | Active site: {"description":"Nucleophile or proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00907","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25010423","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"19193103","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25010423","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
