Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
| D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue TBE A 501 |
| Chain | Residue |
| A | SER91 |
| A | GLN147 |
| A | TYR248 |
| A | ALA345 |
| A | THR346 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | GLU299 |
| A | LYS342 |
| A | THR343 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | PRO192 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue PGE B 502 |
| Chain | Residue |
| B | LYS326 |
| B | PRO327 |
| B | THR329 |
| B | HOH601 |
| C | PRO115 |
| C | GLY130 |
| C | THR132 |
| C | HIS135 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | SER314 |
| B | HIS341 |
| B | LYS342 |
| B | THR343 |
| B | HOH615 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue PEG C 401 |
| Chain | Residue |
| C | TYR177 |
| C | GLU299 |
| C | SER314 |
| C | HIS341 |
| C | LYS342 |
| C | THR343 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue PGE D 502 |
| Chain | Residue |
| D | SER91 |
| D | GLU299 |
| D | SER314 |
| D | ASN316 |
| D | ALA319 |
| D | THR343 |
| D | ASN373 |
| D | TBE501 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 503 |
| Chain | Residue |
| D | ASN36 |
| D | HIS40 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide TBE B 501 and SER B 91 |
| Chain | Residue |
| B | LEU89 |
| B | GLY90 |
| B | VAL92 |
| B | SER93 |
| B | LYS94 |
| B | GLN147 |
| B | TYR177 |
| B | ALA247 |
| B | TYR248 |
| B | LYS342 |
| B | THR343 |
| B | GLY344 |
| B | ALA345 |
| B | THR346 |
| B | GLY347 |
| site_id | AD1 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide TBE C 402 and SER C 91 |
| Chain | Residue |
| C | LEU89 |
| C | GLY90 |
| C | VAL92 |
| C | SER93 |
| C | LYS94 |
| C | GLN147 |
| C | TYR177 |
| C | ASN179 |
| C | ALA247 |
| C | TYR248 |
| C | LYS342 |
| C | THR343 |
| C | GLY344 |
| C | ALA345 |
| C | THR346 |
| C | GLY347 |
| site_id | AD2 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide TBE D 501 and SER D 91 |
| Chain | Residue |
| D | LEU89 |
| D | GLY90 |
| D | VAL92 |
| D | SER93 |
| D | LYS94 |
| D | GLN147 |
| D | TYR177 |
| D | ALA247 |
| D | TYR248 |
| D | LYS342 |
| D | THR343 |
| D | GLY344 |
| D | ALA345 |
| D | THR346 |
| D | GLY347 |
| D | PGE502 |
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 | PHE87-LYS94 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | SER91 | |
| B | SER91 | |
| C | SER91 | |
| D | SER91 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| 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 | SER91 | |
| B | SER91 | |
| C | SER91 | |
| D | SER91 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9 |
| Chain | Residue | Details |
| A | GLN147 | |
| B | GLN147 | |
| C | GLN147 | |
| D | GLN147 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY |
| Chain | Residue | Details |
| A | TYR177 | |
| B | TYR177 | |
| C | TYR177 | |
| D | TYR177 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| 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 | ASN179 | |
| A | ALA345 | |
| B | ASN179 | |
| B | ALA345 | |
| C | ASN179 | |
| C | ALA345 | |
| D | ASN179 | |
| D | ALA345 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0007744|PDB:1KVM |
| Chain | Residue | Details |
| A | ASN370 | |
| B | ASN370 | |
| C | ASN370 | |
| D | ASN370 |
