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 | 6 |
Details | BINDING SITE FOR RESIDUE C21 A 501 |
Chain | Residue |
A | ARG148 |
A | TYR150 |
A | LYS290 |
A | HOH532 |
A | HOH537 |
A | HOH596 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE C21 A 502 |
Chain | Residue |
A | GLN256 |
A | ALA307 |
A | ARG309 |
A | PRO330 |
A | HOH582 |
A | ASN237 |
A | LEU238 |
A | PRO240 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE C21 A 503 |
Chain | Residue |
A | ALA141 |
A | TRP142 |
A | ALA143 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE C21 B 504 |
Chain | Residue |
B | ASN237 |
B | LEU238 |
B | PRO240 |
B | GLN256 |
B | ALA307 |
B | ARG309 |
B | HOH624 |
B | HOH746 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE C21 B 505 |
Chain | Residue |
B | PRO140 |
B | TRP142 |
B | ALA143 |
B | HOH715 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE C21 A 506 |
Chain | Residue |
A | VAL211 |
A | SER212 |
A | TYR221 |
A | THR319 |
A | GLY320 |
A | HOH623 |
A | HOH710 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE C21 B 507 |
Chain | Residue |
B | VAL211 |
B | SER212 |
B | THR319 |
B | GLY320 |
B | HOH631 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE C21 A 508 |
Chain | Residue |
A | PRO297 |
A | LYS299 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE C21 A 509 |
Chain | Residue |
A | ALA231 |
A | ARG232 |
A | GLN235 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE C21 B 510 |
Chain | Residue |
B | LYS24 |
B | ILE48 |
B | LYS342 |
B | C21511 |
B | HOH543 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE C21 B 511 |
Chain | Residue |
B | LYS24 |
B | C21510 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE C21 B 512 |
Chain | Residue |
B | GLY36 |
B | ALA231 |
B | ARG232 |
B | GLN235 |
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
Chain | Residue | Details |
A | SER64 | |
B | SER64 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR150 | |
B | TYR150 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | LYS315 | |
B | LYS315 | |