4WZ5
Crystal structure of P. aeruginosa OXA10
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 |
C | 0005886 | cellular_component | plasma membrane |
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 | 0042597 | cellular_component | periplasmic space |
C | 0046677 | biological_process | response to antibiotic |
C | 0071555 | biological_process | cell wall organization |
D | 0005886 | cellular_component | plasma membrane |
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 | 0042597 | cellular_component | periplasmic space |
D | 0046677 | biological_process | response to antibiotic |
D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | binding site for residue SO4 A 301 |
Chain | Residue |
A | ARG160 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 302 |
Chain | Residue |
A | THR80 |
A | ARG131 |
A | LYS134 |
A | TYR135 |
site_id | AC3 |
Number of Residues | 13 |
Details | binding site for residue 3VU A 303 |
Chain | Residue |
A | VAL117 |
A | LEU155 |
A | GLY207 |
A | PHE208 |
A | SER209 |
A | ARG250 |
A | HOH416 |
A | HOH430 |
A | HOH459 |
A | ALA66 |
A | SER67 |
A | TRP102 |
A | SER115 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 301 |
Chain | Residue |
B | THR80 |
B | ARG131 |
B | LYS134 |
B | TYR135 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue SO4 B 302 |
Chain | Residue |
B | ARG160 |
B | HOH470 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 303 |
Chain | Residue |
B | GLY128 |
B | GLU129 |
B | VAL130 |
B | HOH448 |
site_id | AC7 |
Number of Residues | 14 |
Details | binding site for residue 3VU B 304 |
Chain | Residue |
B | ALA66 |
B | SER67 |
B | TRP102 |
B | SER115 |
B | VAL117 |
B | LEU155 |
B | GLY207 |
B | PHE208 |
B | SER209 |
B | ARG250 |
B | HOH418 |
B | HOH436 |
B | HOH439 |
B | HOH451 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue SO4 C 301 |
Chain | Residue |
B | LYS95 |
C | SER67 |
C | SER115 |
C | LYS205 |
C | THR206 |
C | GLY207 |
C | PHE208 |
C | ARG250 |
C | HOH452 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue SO4 C 302 |
Chain | Residue |
C | TYR63 |
C | LEU64 |
C | VAL219 |
C | HOH472 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue SO4 C 303 |
Chain | Residue |
C | SER181 |
C | LYS182 |
C | HOH457 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue SO4 C 304 |
Chain | Residue |
A | THR107 |
A | ARG109 |
C | PRO198 |
C | GLU227 |
C | GLU229 |
C | HOH440 |
C | HOH464 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue CO2 C 305 |
Chain | Residue |
C | SER67 |
C | LYS70 |
C | VAL117 |
C | PHE120 |
C | TRP154 |
C | LEU155 |
site_id | AD4 |
Number of Residues | 9 |
Details | binding site for residue SO4 D 301 |
Chain | Residue |
A | LYS95 |
D | SER67 |
D | SER115 |
D | LYS205 |
D | THR206 |
D | GLY207 |
D | PHE208 |
D | ARG250 |
D | HOH543 |
site_id | AD5 |
Number of Residues | 9 |
Details | binding site for residue SO4 D 302 |
Chain | Residue |
B | GLU199 |
B | TYR200 |
B | GLU227 |
B | GLU229 |
D | THR107 |
D | ARG109 |
D | GLY110 |
D | HOH460 |
D | HOH530 |
site_id | AD6 |
Number of Residues | 8 |
Details | binding site for residue SO4 D 303 |
Chain | Residue |
B | THR107 |
B | ARG109 |
D | PRO198 |
D | GLU199 |
D | TYR200 |
D | GLU227 |
D | GLU229 |
D | HOH448 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue SO4 D 304 |
Chain | Residue |
D | LYS182 |
B | HOH477 |
D | SER181 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue CO2 D 305 |
Chain | Residue |
D | SER67 |
D | LYS70 |
D | VAL117 |
D | PHE120 |
D | TRP154 |
D | LEU155 |
D | HOH442 |
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 |
C | PRO65-ILE75 | |
A | PRO65-ILE75 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PubMed","id":"11724923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K54","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WGI","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WGI","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"11188693","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11724923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K4E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K4F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K54","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K55","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K56","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K57","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RL3","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |