6NVY
Crystal structure of penicillin G acylase from Bacillus thermotolerans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 301 |
| Chain | Residue |
| A | GLU53 |
| A | ASP136 |
| A | HOH404 |
| A | HOH417 |
| A | HOH428 |
| A | HOH456 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 601 |
| Chain | Residue |
| B | ASP76 |
| B | GLU256 |
| B | HOH751 |
| A | GLU154 |
| B | ASN73 |
| B | THR75 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 602 |
| Chain | Residue |
| B | ASP336 |
| B | ASN338 |
| B | ASP340 |
| B | LEU342 |
| B | ASP344 |
| B | HOH875 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue CA B 603 |
| Chain | Residue |
| B | GLU8 |
| B | ASP9 |
| B | ARG189 |
| B | CA605 |
| B | HOH849 |
| B | HOH858 |
| B | HOH925 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 604 |
| Chain | Residue |
| B | LYS12 |
| B | ASP284 |
| B | GLU287 |
| B | HOH732 |
| B | HOH784 |
| B | HOH865 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue CA B 605 |
| Chain | Residue |
| B | GLU8 |
| B | ASP9 |
| B | GLY14 |
| B | CA603 |
| B | HOH761 |
| B | HOH912 |
| B | HOH950 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 606 |
| Chain | Residue |
| A | ARG72 |
| A | TYR76 |
| B | ARG102 |
| B | GLU104 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue CA C 301 |
| Chain | Residue |
| C | GLU53 |
| C | ASP136 |
| C | HOH401 |
| C | HOH412 |
| C | HOH415 |
| C | HOH419 |
| C | HOH454 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 601 |
| Chain | Residue |
| C | GLU154 |
| D | ASN73 |
| D | THR75 |
| D | ASP76 |
| D | GLU256 |
| D | HOH739 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 602 |
| Chain | Residue |
| D | ASP336 |
| D | ASN338 |
| D | ASP340 |
| D | LEU342 |
| D | ASP344 |
| D | HOH748 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 603 |
| Chain | Residue |
| D | GLU8 |
| D | ASP9 |
| D | ARG189 |
| D | CA605 |
| D | HOH827 |
| D | HOH913 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 604 |
| Chain | Residue |
| D | LYS12 |
| D | ASP284 |
| D | HOH708 |
| D | HOH747 |
| D | HOH849 |
| D | HOH960 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue CA D 605 |
| Chain | Residue |
| D | GLU8 |
| D | ASP9 |
| D | GLY14 |
| D | CA603 |
| D | HOH749 |
| D | HOH853 |
| D | HOH903 |
Functional Information from PROSITE/UniProt
| site_id | PS00165 |
| Number of Residues | 15 |
| Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. DhrygaTLAYKILAG |
| Chain | Residue | Details |
| B | ASP379-GLY393 |
| site_id | PS00430 |
| Number of Residues | 111 |
| Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. snamivgedksktgnallfsgpqvgfvapgflyevglhapgfdmegsgfigypfimfgankhialtatagygnvtdifeeklhpndptqyfykgewremekrt............ETFTVRGE |
| Chain | Residue | Details |
| B | SER1-GLU111 |
