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: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 |