4K4A
X-ray crystal structure of E. coli YdiI complexed with phenacyl-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 | 29 |
| Details | BINDING SITE FOR RESIDUE 0FQ A 201 |
| Chain | Residue |
| A | GLN48 |
| A | HOH302 |
| A | HOH303 |
| A | HOH315 |
| A | HOH340 |
| A | HOH386 |
| A | HOH413 |
| A | HOH429 |
| A | HOH436 |
| B | GLU63 |
| B | SER67 |
| A | PRO49 |
| B | VAL81 |
| B | GLY82 |
| C | LYS4 |
| C | SER109 |
| D | HIS106 |
| D | GLY108 |
| D | SER109 |
| D | ARG110 |
| D | HIS111 |
| D | HOH301 |
| A | LEU53 |
| A | HIS54 |
| A | GLY55 |
| A | HIS89 |
| A | VAL90 |
| A | ARG91 |
| A | SER92 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE 0FQ B 201 |
| Chain | Residue |
| A | GLU77 |
| A | LYS79 |
| B | HIS106 |
| B | GLY108 |
| B | SER109 |
| B | ARG110 |
| B | HIS111 |
| B | HOH310 |
| B | HOH344 |
| B | HOH417 |
| C | GLN48 |
| C | PRO49 |
| C | LEU53 |
| C | HIS54 |
| C | GLY55 |
| C | HIS89 |
| C | VAL90 |
| C | ARG91 |
| C | SER92 |
| D | GLU63 |
| D | SER67 |
| D | GLY82 |
| D | LEU83 |
| D | LEU136 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE 0FQ C 201 |
| Chain | Residue |
| A | GLU63 |
| A | SER67 |
| A | GLY82 |
| A | LEU83 |
| A | LEU136 |
| B | GLN48 |
| B | PRO49 |
| B | LEU53 |
| B | HIS54 |
| B | GLY55 |
| B | HIS89 |
| B | VAL90 |
| B | ARG91 |
| B | SER92 |
| B | ARG110 |
| C | HIS106 |
| C | GLY108 |
| C | SER109 |
| C | ARG110 |
| C | HIS111 |
| C | HOH317 |
| C | HOH323 |
| C | HOH391 |
| C | HOH392 |
| C | HOH397 |
| C | HOH398 |
| C | HOH426 |
| C | HOH441 |
| C | HOH442 |
| D | SER109 |
| D | ARG110 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE 0FQ D 201 |
| Chain | Residue |
| D | GLN48 |
| D | PRO49 |
| D | LEU53 |
| D | HIS54 |
| D | GLY55 |
| D | HIS89 |
| D | VAL90 |
| D | ARG91 |
| D | SER92 |
| D | HOH305 |
| D | HOH309 |
| D | HOH313 |
| D | HOH343 |
| D | HOH369 |
| D | HOH374 |
| D | HOH389 |
| D | HOH402 |
| A | HIS106 |
| A | GLY108 |
| A | SER109 |
| A | ARG110 |
| A | HIS111 |
| A | HOH414 |
| A | HOH449 |
| B | GLU77 |
| B | HOH420 |
| C | GLU63 |
| C | SER67 |
| C | VAL81 |
| C | GLY82 |
| C | LEU83 |
| C | LEU136 |
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 |
