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 | ACT_SITE: Nucleophile or proton acceptor => ECO:0000255|HAMAP-Rule:MF_01936, ECO:0000303|PubMed:25010423 |
Chain | Residue | Details |
A | GLU63 | |
B | GLU63 | |
C | GLU63 | |
D | GLU63 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01936, ECO:0000269|PubMed:25010423 |
Chain | Residue | Details |
B | HIS89 | |
B | HIS106 | |
C | GLY82 | |
C | HIS89 | |
C | HIS106 | |
D | GLY82 | |
D | HIS89 | |
D | HIS106 | |
A | GLY82 | |
A | HIS89 | |
A | HIS106 | |
B | GLY82 |