4E3N
Crystal structure of AmpC beta-lactamase in complex with a 2-trifluoromethyl-4-tetrazolyl benzene sulfonamide boronic acid inhibitor
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0042597 | cellular_component | periplasmic space |
A | 0046677 | biological_process | response to antibiotic |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0042597 | cellular_component | periplasmic space |
B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 0NE A 401 |
Chain | Residue |
A | SER64 |
A | HOH769 |
A | HOH770 |
A | HOH771 |
A | HOH794 |
A | TYR150 |
A | ASN152 |
A | VAL211 |
A | SER212 |
A | ALA318 |
A | THR319 |
A | GLY320 |
A | ASN343 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 402 |
Chain | Residue |
A | GLN261 |
A | GLY263 |
A | PRO297 |
B | TYR45 |
B | LYS51 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 0NE B 401 |
Chain | Residue |
B | SER64 |
B | GLN120 |
B | TYR150 |
B | ASN152 |
B | VAL211 |
B | SER212 |
B | ALA318 |
B | THR319 |
B | GLY320 |
B | HOH738 |
B | HOH739 |
B | HOH741 |
B | HOH743 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 B 402 |
Chain | Residue |
A | PHE41 |
A | THR42 |
A | HOH647 |
A | HOH649 |
B | GLY116 |
B | ALA141 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 B 403 |
Chain | Residue |
A | ARG133 |
A | HIS186 |
B | LYS290 |
Functional Information from PROSITE/UniProt
site_id | PS00336 |
Number of Residues | 8 |
Details | BETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK |
Chain | Residue | Details |
A | PHE60-LYS67 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:11478888, ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:16506777, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201, ECO:0000269|DOI:10.1021/ja001676x |
Chain | Residue | Details |
A | SER64 | |
B | SER64 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:2FFY |
Chain | Residue | Details |
A | SER64 | |
B | SER64 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9 |
Chain | Residue | Details |
A | GLN120 | |
B | GLN120 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY |
Chain | Residue | Details |
A | TYR150 | |
B | TYR150 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9, ECO:0007744|PDB:2FFY |
Chain | Residue | Details |
A | ASN152 | |
A | ALA318 | |
B | ASN152 | |
B | ALA318 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0007744|PDB:1KVM |
Chain | Residue | Details |
A | ASN343 | |
B | ASN343 |