4K49
X-ray crystal structure of E. coli YdiI complexed with 2,4-dihydroxyphenacyl CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0009234 | biological_process | menaquinone biosynthetic process |
| A | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016790 | molecular_function | thiolester hydrolase activity |
| A | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0009234 | biological_process | menaquinone biosynthetic process |
| B | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016790 | molecular_function | thiolester hydrolase activity |
| B | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0009234 | biological_process | menaquinone biosynthetic process |
| C | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016790 | molecular_function | thiolester hydrolase activity |
| C | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0009234 | biological_process | menaquinone biosynthetic process |
| D | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016790 | molecular_function | thiolester hydrolase activity |
| D | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE HFQ C 201 |
| Chain | Residue |
| A | SER109 |
| B | LEU136 |
| B | HOH342 |
| C | GLN48 |
| C | PRO49 |
| C | LEU53 |
| C | HIS54 |
| C | GLY55 |
| C | HIS89 |
| C | VAL90 |
| C | ARG91 |
| A | ARG110 |
| C | SER92 |
| C | ARG110 |
| C | HOH310 |
| C | HOH315 |
| C | HOH324 |
| C | HOH349 |
| C | HOH359 |
| C | HOH386 |
| C | HOH423 |
| D | HIS106 |
| A | HOH354 |
| D | GLY108 |
| D | SER109 |
| D | ARG110 |
| D | HIS111 |
| B | GLU63 |
| B | SER67 |
| B | VAL68 |
| B | LYS79 |
| B | VAL80 |
| B | GLY82 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE HFQ B 201 |
| Chain | Residue |
| A | HIS106 |
| A | GLY108 |
| A | SER109 |
| A | ARG110 |
| A | HIS111 |
| A | HOH301 |
| B | GLN48 |
| B | PRO49 |
| B | LEU53 |
| B | HIS54 |
| B | GLY55 |
| B | HIS89 |
| B | VAL90 |
| B | ARG91 |
| B | SER92 |
| B | HOH303 |
| B | HOH309 |
| B | HOH311 |
| B | HOH324 |
| B | HOH347 |
| B | HOH349 |
| B | HOH361 |
| B | HOH380 |
| B | HOH431 |
| B | HOH451 |
| B | HOH481 |
| C | GLU63 |
| C | SER67 |
| C | VAL80 |
| C | GLY82 |
| D | LYS4 |
| D | SER109 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE HFQ D 201 |
| Chain | Residue |
| A | GLU63 |
| A | SER67 |
| A | GLY82 |
| A | LEU136 |
| B | GLU77 |
| B | LYS79 |
| C | HIS106 |
| C | GLY108 |
| C | SER109 |
| C | ARG110 |
| C | HIS111 |
| D | GLN48 |
| D | PRO49 |
| D | LEU53 |
| D | HIS54 |
| D | GLY55 |
| D | HIS89 |
| D | VAL90 |
| D | ARG91 |
| D | SER92 |
| D | ARG94 |
| D | HOH313 |
| D | HOH316 |
| D | HOH333 |
| D | HOH352 |
| D | HOH353 |
| D | HOH398 |
| D | HOH402 |
| D | HOH408 |
| D | HOH428 |
| D | HOH448 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE HFQ A 201 |
| Chain | Residue |
| A | HIS54 |
| A | GLY55 |
| A | HIS89 |
| A | VAL90 |
| A | ARG91 |
| A | SER92 |
| A | HOH304 |
| A | HOH310 |
| A | HOH311 |
| A | HOH319 |
| A | HOH359 |
| A | HOH361 |
| A | HOH376 |
| A | HOH378 |
| A | HOH382 |
| B | HIS106 |
| B | GLY108 |
| B | SER109 |
| B | ARG110 |
| B | HIS111 |
| B | HOH462 |
| C | GLU77 |
| D | GLU63 |
| D | SER67 |
| D | VAL68 |
| D | VAL80 |
| D | GLY82 |
| D | LEU136 |
| A | GLN48 |
| A | PRO49 |
| A | LEU53 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile or proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01936","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25010423","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01936","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25010423","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
