6YPD
Crystal structure of AmpC from E. coli with Cyclic Boronate 3 (CB3 / APC308)
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue KL8 A 401 |
| Chain | Residue |
| A | SER64 |
| A | GLY317 |
| A | ALA318 |
| A | ASN346 |
| A | HOH502 |
| A | HOH703 |
| A | HOH745 |
| A | GLN120 |
| A | TYR150 |
| A | ASN152 |
| A | VAL211 |
| A | TYR221 |
| A | ASN289 |
| A | LYS315 |
| A | THR316 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue PEG A 402 |
| Chain | Residue |
| A | LEU131 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 403 |
| Chain | Residue |
| A | ASP281 |
| A | ILE284 |
| A | ASP351 |
| A | GLN355 |
| A | EDO404 |
| A | HOH802 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | LYS246 |
| A | GLN250 |
| A | DMS403 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue PEG A 405 |
| Chain | Residue |
| A | LYS24 |
| A | TYR40 |
| A | THR42 |
| A | THR55 |
| A | GLN56 |
| A | HOH538 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | ASN343 |
| A | PRO345 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 407 |
| Chain | Residue |
| A | HIS13 |
| A | HIS13 |
| A | HIS13 |
| A | ZN408 |
| A | ZN408 |
| A | ZN408 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 408 |
| Chain | Residue |
| A | HIS13 |
| A | HIS13 |
| A | HIS13 |
| A | CL407 |
| A | CL407 |
| A | CL407 |
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 | 1 |
| 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:35486701, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201, ECO:0000269|DOI:10.1021/ja001676x |
| Chain | Residue | Details |
| A | SER64 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| 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 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9 |
| Chain | Residue | Details |
| A | GLN120 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY |
| Chain | Residue | Details |
| A | TYR150 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0007744|PDB:1KVM |
| Chain | Residue | Details |
| A | ASN343 |
