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 | 4 |
Details | binding site for residue EDO A 301 |
Chain | Residue |
A | ASN143 |
A | ASN145 |
A | HOH448 |
A | HOH503 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | GLU224 |
A | GLU226 |
A | HOH511 |
C | THR107 |
site_id | AC3 |
Number of Residues | 20 |
Details | binding site for residue DWZ A 303 |
Chain | Residue |
A | SER67 |
A | KCX70 |
A | MET99 |
A | GLN101 |
A | TRP102 |
A | GLN113 |
A | VAL114 |
A | SER115 |
A | VAL117 |
A | LEU155 |
A | GLY207 |
A | TRP208 |
A | ARG247 |
A | HOH416 |
A | HOH437 |
A | HOH449 |
A | HOH469 |
A | HOH491 |
C | PRO198 |
A | ALA66 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | SER181 |
A | LYS182 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue EDO A 305 |
Chain | Residue |
A | ARG160 |
A | HOH470 |
A | HOH522 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO B 301 |
Chain | Residue |
B | ALA98 |
B | HOH417 |
B | HOH585 |
B | HOH586 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
A | LYS84 |
A | ASN85 |
A | HOH429 |
B | THR23 |
B | GLU24 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
B | ASN143 |
B | ASN145 |
B | HOH449 |
B | HOH474 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue EDO B 305 |
Chain | Residue |
B | ARG160 |
B | HOH476 |
B | HOH531 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue EDO C 301 |
Chain | Residue |
C | ALA36 |
C | VAL37 |
C | ASN38 |
C | HOH402 |
D | ASP55 |
D | ALA57 |
D | ARG58 |
D | LYS61 |
D | HOH410 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue EDO D 301 |
Chain | Residue |
B | THR107 |
B | HOH468 |
D | GLU199 |
D | GLU224 |
D | GLU226 |
D | HOH445 |
D | HOH553 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue EDO D 302 |
Chain | Residue |
C | THR252 |
D | ARG131 |
D | TYR135 |
D | HOH429 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue EDO D 304 |
Chain | Residue |
D | LYS84 |
D | ASN85 |
D | HOH493 |
site_id | AD5 |
Number of Residues | 25 |
Details | binding site for Di-peptide DWZ B 302 and SER B 67 |
Chain | Residue |
B | PRO65 |
B | ALA66 |
B | THR68 |
B | PHE69 |
B | KCX70 |
B | MET99 |
B | GLN101 |
B | TRP102 |
B | GLN113 |
B | VAL114 |
B | SER115 |
B | VAL117 |
B | LEU155 |
B | LYS205 |
B | THR206 |
B | GLY207 |
B | TRP208 |
B | MET210 |
B | ARG247 |
B | HOH408 |
B | HOH416 |
B | HOH443 |
B | HOH523 |
B | HOH525 |
D | PRO198 |
site_id | AD6 |
Number of Residues | 23 |
Details | binding site for Di-peptide DWZ C 302 and SER C 67 |
Chain | Residue |
C | THR68 |
C | PHE69 |
C | KCX70 |
C | MET99 |
C | GLN101 |
C | VAL114 |
C | SER115 |
C | VAL117 |
C | LEU155 |
C | LYS205 |
C | THR206 |
C | GLY207 |
C | TRP208 |
C | MET210 |
C | LEU244 |
C | ARG247 |
C | HOH401 |
C | HOH418 |
C | HOH436 |
C | HOH493 |
C | HOH545 |
C | PRO65 |
C | ALA66 |
site_id | AD7 |
Number of Residues | 21 |
Details | binding site for Di-peptide DWZ D 303 and SER D 67 |
Chain | Residue |
D | PRO65 |
D | ALA66 |
D | THR68 |
D | PHE69 |
D | KCX70 |
D | MET99 |
D | GLN101 |
D | VAL114 |
D | SER115 |
D | VAL117 |
D | LEU155 |
D | LYS205 |
D | THR206 |
D | GLY207 |
D | TRP208 |
D | MET210 |
D | ARG247 |
D | HOH407 |
D | HOH422 |
D | HOH489 |
D | HOH522 |
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 | |