Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008658 | molecular_function | penicillin binding |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
A | 0046677 | biological_process | response to antibiotic |
A | 0046872 | molecular_function | metal ion binding |
A | 0071555 | biological_process | cell wall organization |
B | 0008658 | molecular_function | penicillin binding |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
B | 0046677 | biological_process | response to antibiotic |
B | 0046872 | molecular_function | metal ion binding |
B | 0071555 | biological_process | cell wall organization |
C | 0008658 | molecular_function | penicillin binding |
C | 0008800 | molecular_function | beta-lactamase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0017001 | biological_process | antibiotic catabolic process |
C | 0046677 | biological_process | response to antibiotic |
C | 0046872 | molecular_function | metal ion binding |
C | 0071555 | biological_process | cell wall organization |
D | 0008658 | molecular_function | penicillin binding |
D | 0008800 | molecular_function | beta-lactamase activity |
D | 0016787 | molecular_function | hydrolase activity |
D | 0017001 | biological_process | antibiotic catabolic process |
D | 0046677 | biological_process | response to antibiotic |
D | 0046872 | molecular_function | metal ion binding |
D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue 2RG A 301 |
Chain | Residue |
A | ALA66 |
A | HOH536 |
A | SER67 |
A | SER115 |
A | VAL117 |
A | LEU155 |
A | THR206 |
A | GLY207 |
A | TRP208 |
A | ARG247 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | ASN85 |
A | HIS87 |
A | HOH405 |
D | LEU175 |
D | ASN176 |
D | LYS182 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue EDO B 302 |
Chain | Residue |
B | GLN113 |
B | THR194 |
B | SER204 |
B | LYS205 |
B | THR206 |
B | HOH412 |
B | HOH435 |
B | HOH466 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | VAL89 |
B | ASP105 |
B | HOH516 |
C | THR227 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue EDO C 302 |
Chain | Residue |
B | LEU186 |
B | LYS189 |
B | GLU190 |
C | GLU86 |
C | GLU190 |
C | HOH513 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue EDO C 303 |
Chain | Residue |
B | GLU224 |
B | GLU226 |
B | HOH482 |
C | THR107 |
C | ARG109 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue EDO C 304 |
Chain | Residue |
C | GLU195 |
C | TYR200 |
C | VAL202 |
C | TRP219 |
C | THR252 |
C | ILE261 |
C | HOH516 |
C | HOH594 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue EDO C 305 |
Chain | Residue |
C | GLU126 |
D | GLU256 |
D | GLY259 |
D | ILE261 |
D | GLY262 |
D | HOH510 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue EDO C 306 |
Chain | Residue |
B | THR107 |
B | ARG109 |
C | GLU199 |
C | GLU224 |
C | GLU226 |
C | HOH502 |
C | HOH566 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue EDO C 307 |
Chain | Residue |
C | ALA36 |
C | ASN38 |
C | HOH411 |
D | ARG58 |
D | LYS61 |
D | HOH409 |
D | HOH537 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue EDO D 302 |
Chain | Residue |
A | THR107 |
A | ARG109 |
D | GLU199 |
D | GLU224 |
D | GLU226 |
D | HOH468 |
D | HOH503 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue EDO D 303 |
Chain | Residue |
A | HOH499 |
D | THR107 |
D | ARG109 |
D | EDO306 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue EDO D 304 |
Chain | Residue |
D | GLY149 |
D | ILE150 |
D | HOH512 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue EDO D 305 |
Chain | Residue |
D | ARG131 |
D | TYR135 |
D | HOH509 |
D | HOH555 |
D | HOH562 |
site_id | AD6 |
Number of Residues | 7 |
Details | binding site for residue EDO D 306 |
Chain | Residue |
A | PRO198 |
A | HOH412 |
D | ARG104 |
D | GLY110 |
D | 2RG301 |
D | EDO303 |
D | HOH558 |
site_id | AD7 |
Number of Residues | 15 |
Details | binding site for Di-peptide 2RG B 301 and SER B 67 |
Chain | Residue |
B | SER115 |
B | VAL117 |
B | LEU155 |
B | LYS205 |
B | THR206 |
B | GLY207 |
B | TRP208 |
B | ARG247 |
B | HOH559 |
B | PRO65 |
B | ALA66 |
B | THR68 |
B | PHE69 |
B | KCX70 |
B | GLN101 |
site_id | AD8 |
Number of Residues | 20 |
Details | binding site for Di-peptide 2RG C 301 and SER C 67 |
Chain | Residue |
B | PRO198 |
C | PRO65 |
C | ALA66 |
C | THR68 |
C | PHE69 |
C | KCX70 |
C | MET99 |
C | GLN101 |
C | ARG104 |
C | VAL114 |
C | SER115 |
C | VAL117 |
C | LEU155 |
C | LYS205 |
C | THR206 |
C | GLY207 |
C | TRP208 |
C | ARG247 |
C | HOH418 |
C | HOH583 |
site_id | AD9 |
Number of Residues | 20 |
Details | binding site for Di-peptide 2RG D 301 and SER D 67 |
Chain | Residue |
A | PRO198 |
D | PRO65 |
D | ALA66 |
D | THR68 |
D | PHE69 |
D | KCX70 |
D | MET99 |
D | GLN101 |
D | ARG104 |
D | VAL114 |
D | SER115 |
D | VAL117 |
D | LEU155 |
D | LYS205 |
D | THR206 |
D | GLY207 |
D | TRP208 |
D | ARG247 |
D | EDO306 |
D | HOH402 |
Functional Information from PROSITE/UniProt
site_id | PS00337 |
Number of Residues | 11 |
Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnAI |
Chain | Residue | Details |
A | PRO65-ILE75 | |