Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
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 | 0042597 | cellular_component | periplasmic space |
A | 0046677 | biological_process | response to antibiotic |
A | 0071555 | biological_process | cell wall organization |
B | 0005886 | cellular_component | plasma membrane |
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 | 0042597 | cellular_component | periplasmic space |
B | 0046677 | biological_process | response to antibiotic |
B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | binding site for residue NXL A 301 |
Chain | Residue |
A | ALA66 |
A | ARG250 |
A | HOH413 |
A | HOH503 |
A | HOH550 |
A | HOH562 |
A | HOH596 |
A | SER67 |
A | MET99 |
A | SER115 |
A | VAL117 |
A | LYS205 |
A | THR206 |
A | GLY207 |
A | PHE208 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue NA A 302 |
Chain | Residue |
A | ARG250 |
A | HOH695 |
A | HOH713 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CO2 A 303 |
Chain | Residue |
A | SER67 |
A | LYS70 |
A | PHE120 |
A | TRP154 |
A | HOH413 |
A | HOH553 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue GOL A 304 |
Chain | Residue |
A | TRP92 |
A | GLY94 |
A | PRO96 |
A | GLU103 |
A | ASN145 |
A | HOH410 |
A | HOH510 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue GOL A 305 |
Chain | Residue |
A | LYS138 |
A | PHE139 |
A | SER140 |
A | GLU168 |
A | SER172 |
A | LEU178 |
A | HOH407 |
A | HOH446 |
A | HOH551 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue NA B 302 |
Chain | Residue |
B | LYS70 |
B | TRP154 |
B | HOH532 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue GOL B 303 |
Chain | Residue |
A | ALA197 |
A | TYR200 |
A | GLU229 |
B | THR107 |
B | ARG109 |
B | HOH433 |
site_id | AC8 |
Number of Residues | 15 |
Details | binding site for Di-peptide NXL B 301 and SER B 67 |
Chain | Residue |
B | PRO65 |
B | ALA66 |
B | THR68 |
B | PHE69 |
B | LYS70 |
B | SER115 |
B | VAL117 |
B | LEU155 |
B | LYS205 |
B | THR206 |
B | GLY207 |
B | PHE208 |
B | ARG250 |
B | HOH405 |
B | HOH592 |
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 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER67 | |
B | SER67 | |
Chain | Residue | Details |
A | SER115 | |
A | THR206 | |
A | PHE208 | |
A | ARG250 | |
B | SER115 | |
B | THR206 | |
B | PHE208 | |
B | ARG250 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:11188693, ECO:0000269|PubMed:11724923, ECO:0000269|PubMed:19860471, ECO:0007744|PDB:1E4D, ECO:0007744|PDB:1K4E, ECO:0007744|PDB:1K4F, ECO:0007744|PDB:1K54, ECO:0007744|PDB:1K55, ECO:0007744|PDB:1K56, ECO:0007744|PDB:1K57, ECO:0007744|PDB:1K6S, ECO:0007744|PDB:2RL3 |
Chain | Residue | Details |
A | LYS70 | |
B | LYS70 | |