5D6O
Orthorhombic Crystal Structure of an acetylester hydrolase from Corynebacterium glutamicum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004414 | molecular_function | homoserine O-acetyltransferase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004414 | molecular_function | homoserine O-acetyltransferase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0016787 | molecular_function | hydrolase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004414 | molecular_function | homoserine O-acetyltransferase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| C | 0016787 | molecular_function | hydrolase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004414 | molecular_function | homoserine O-acetyltransferase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| D | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 401 |
| Chain | Residue |
| A | TRP57 |
| A | TYR58 |
| A | SER142 |
| A | MET143 |
| A | GOL407 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 402 |
| Chain | Residue |
| A | THR61 |
| A | THR64 |
| A | GOL410 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | HOH534 |
| A | HOH540 |
| A | HOH572 |
| A | HOH672 |
| A | HOH892 |
| A | HOH905 |
| A | HIS74 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | LEU2 |
| A | ASN4 |
| A | TYR7 |
| A | GLY92 |
| A | SER96 |
| A | ALA98 |
| A | ASN99 |
| A | HOH614 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | GLU227 |
| A | ARG230 |
| A | GLU235 |
| A | HOH513 |
| A | HOH730 |
| A | HOH760 |
| B | GLN226 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | PRO14 |
| A | TYR15 |
| A | GLU16 |
| A | THR40 |
| A | HOH588 |
| C | ARG127 |
| C | THR133 |
| C | HOH665 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 407 |
| Chain | Residue |
| A | TRP57 |
| A | TYR58 |
| A | SER59 |
| A | SER142 |
| A | TRP214 |
| A | HIS325 |
| A | LEU326 |
| A | PHE329 |
| A | CL401 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 408 |
| Chain | Residue |
| A | ARG127 |
| A | HOH542 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 409 |
| Chain | Residue |
| A | GLY13 |
| A | PRO14 |
| A | THR40 |
| A | PHE66 |
| A | HOH573 |
| A | HOH580 |
| A | HOH751 |
| C | HOH665 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 410 |
| Chain | Residue |
| A | GLN63 |
| A | THR64 |
| A | CL402 |
| A | HOH510 |
| A | HOH530 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 411 |
| Chain | Residue |
| A | GLY233 |
| A | GLU235 |
| A | ALA306 |
| A | LEU310 |
| A | HOH501 |
| A | HOH546 |
| A | HOH615 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 401 |
| Chain | Residue |
| B | TRP57 |
| B | TYR58 |
| B | SER142 |
| B | MET143 |
| B | HOH597 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 402 |
| Chain | Residue |
| B | THR61 |
| B | THR64 |
| B | HOH700 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| B | HIS74 |
| B | HOH580 |
| B | HOH599 |
| B | HOH624 |
| B | HOH715 |
| B | HOH894 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 404 |
| Chain | Residue |
| B | PRO97 |
| B | MET107 |
| B | SER108 |
| B | PHE110 |
| B | ASN255 |
| B | ASN259 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 405 |
| Chain | Residue |
| B | LEU2 |
| B | ASN4 |
| B | TYR7 |
| B | GLY92 |
| B | ALA98 |
| B | ASN99 |
| B | HOH535 |
| site_id | AD8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 406 |
| Chain | Residue |
| A | ASP243 |
| A | HOH613 |
| B | LYS225 |
| B | GLU227 |
| B | HOH741 |
| A | PRO173 |
| A | GLU235 |
| A | SER239 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue CL C 401 |
| Chain | Residue |
| C | TRP57 |
| C | TYR58 |
| C | SER142 |
| C | MET143 |
| C | GOL404 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 402 |
| Chain | Residue |
| C | GLY60 |
| C | THR61 |
| C | THR64 |
| C | HOH676 |
| site_id | AE2 |
| Number of Residues | 7 |
| Details | binding site for residue MG C 403 |
| Chain | Residue |
| C | ASP73 |
| C | HIS74 |
| C | HOH519 |
| C | HOH556 |
| C | HOH580 |
| C | HOH718 |
| C | HOH726 |
| site_id | AE3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 404 |
| Chain | Residue |
| C | TRP57 |
| C | TYR58 |
| C | SER142 |
| C | HIS325 |
| C | LEU326 |
| C | PHE329 |
| C | CL401 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 405 |
| Chain | Residue |
| C | ARG114 |
| C | HIS266 |
| C | ASP268 |
| C | ARG271 |
| C | HOH605 |
| C | HOH624 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue CL D 401 |
| Chain | Residue |
| D | TRP57 |
| D | TYR58 |
| D | SER142 |
| D | MET143 |
| D | GOL406 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 402 |
| Chain | Residue |
| D | GLY60 |
| D | THR61 |
| D | THR64 |
| D | HOH666 |
| site_id | AE7 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 403 |
| Chain | Residue |
| D | HIS74 |
| D | HOH549 |
| D | HOH605 |
| D | HOH678 |
| D | HOH684 |
| D | HOH911 |
| site_id | AE8 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 404 |
| Chain | Residue |
| D | VAL11 |
| D | GLN63 |
| D | HOH810 |
| D | HOH823 |
| D | HOH973 |
| site_id | AE9 |
| Number of Residues | 7 |
| Details | binding site for residue GOL D 405 |
| Chain | Residue |
| C | PRO173 |
| C | LEU234 |
| C | GLU235 |
| C | SER239 |
| D | LYS225 |
| D | GLU227 |
| D | HOH676 |
| site_id | AF1 |
| Number of Residues | 9 |
| Details | binding site for residue GOL D 406 |
| Chain | Residue |
| D | TRP57 |
| D | TYR58 |
| D | SER59 |
| D | SER142 |
| D | TRP214 |
| D | HIS325 |
| D | LEU326 |
| D | PHE329 |
| D | CL401 |
| site_id | AF2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 407 |
| Chain | Residue |
| D | PRO97 |
| D | MET107 |
| D | PHE110 |
| D | ASN255 |
| D | ASN259 |
| D | HOH631 |
| site_id | AF3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL D 408 |
| Chain | Residue |
| C | LEU2 |
| C | ASN4 |
| C | TYR7 |
| C | GLY92 |
| C | ALA98 |
| C | ASN99 |
| C | ASP253 |
| D | HOH511 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:26787467 |
| Chain | Residue | Details |
| A | SER142 | |
| B | SER142 | |
| C | SER142 | |
| D | SER142 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:26787467 |
| Chain | Residue | Details |
| A | ASP296 | |
| A | HIS325 | |
| B | ASP296 | |
| B | HIS325 | |
| C | ASP296 | |
| C | HIS325 | |
| D | ASP296 | |
| D | HIS325 |
