Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 401 |
| Chain | Residue |
| A | HIS116 |
| A | HIS118 |
| A | HIS196 |
| A | CU402 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 402 |
| Chain | Residue |
| A | ASP120 |
| A | HIS121 |
| A | HIS263 |
| A | CU401 |
| A | HOH411 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 403 |
| Chain | Residue |
| A | HIS51 |
| A | HIS51 |
| A | PHN410 |
| A | PHN410 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU B 401 |
| Chain | Residue |
| B | HIS116 |
| B | HIS118 |
| B | HIS196 |
| B | CU402 |
| B | HOH411 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU B 402 |
| Chain | Residue |
| B | ASP120 |
| B | HIS121 |
| B | HIS263 |
| B | CU401 |
| B | HOH587 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 403 |
| Chain | Residue |
| B | HIS51 |
| B | HIS51 |
| B | PHN410 |
| B | PHN410 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1 |
| Chain | Residue |
| A | ARG172 |
| A | VAL179 |
| A | ILE180 |
| A | THR181 |
| A | HOH477 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2 |
| Chain | Residue |
| B | ARG172 |
| B | ILE180 |
| B | THR181 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3 |
| Chain | Residue |
| A | ARG252 |
| A | LYS297 |
| A | HOH539 |
| B | ARG209 |
| B | ALA275 |
| B | ARG276 |
| B | ALA289 |
| B | GLY290 |
| B | ALA291 |
| B | HOH529 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 4 |
| Chain | Residue |
| A | ARG209 |
| A | ALA275 |
| A | ARG276 |
| A | ALA289 |
| A | GLY290 |
| A | ALA291 |
| A | HOH458 |
| A | HOH553 |
| B | ARG252 |
| B | LYS297 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 5 |
| Chain | Residue |
| B | ARG102 |
| B | PHN410 |
| B | HOH511 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 6 |
| Chain | Residue |
| A | TRP53 |
| A | ARG102 |
| A | ASN210 |
| A | GLY211 |
| A | HOH612 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PHN A 410 |
| Chain | Residue |
| A | HIS51 |
| A | HIS51 |
| A | GLY183 |
| A | GLY183 |
| A | THR206 |
| A | THR208 |
| A | THR208 |
| A | CU403 |
| A | CU403 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PHN B 410 |
| Chain | Residue |
| B | SO45 |
| B | ASP50 |
| B | HIS51 |
| B | HIS51 |
| B | THR76 |
| B | PRO77 |
| B | THR208 |
| B | CU403 |
| B | CU403 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 7 |
| Chain | Residue |
| A | ARG276 |
| A | HOH551 |
| B | PHE248 |
| B | ALA249 |
| B | ARG252 |
| B | ALA300 |
| B | ASP301 |
| B | GLU304 |
| B | HOH605 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 8 |
| Chain | Residue |
| A | PHE248 |
| A | ALA249 |
| A | ARG252 |
| A | ALA300 |
| A | ASP301 |
| A | GLU304 |
| A | HOH538 |
| B | ARG276 |
Functional Information from PROSITE/UniProt
| site_id | PS00743 |
| Number of Residues | 21 |
| Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. LlSHaHADhaGPvaelkrrtG |
| Chain | Residue | Details |
| A | LEU113-GLY133 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17999929","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9811546","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P25910","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9811546","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qh5 |
| Chain | Residue | Details |
| A | ASP120 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qh5 |
| Chain | Residue | Details |
| B | ASP120 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 258 |
| Chain | Residue | Details |
| A | HIS116 | metal ligand |
| A | HIS118 | metal ligand |
| A | ASP120 | metal ligand |
| A | HIS121 | metal ligand |
| A | HIS196 | metal ligand |
| A | TYR229 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS263 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 258 |
| Chain | Residue | Details |
| B | HIS116 | metal ligand |
| B | HIS118 | metal ligand |
| B | ASP120 | metal ligand |
| B | HIS121 | metal ligand |
| B | HIS196 | metal ligand |
| B | TYR229 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS263 | metal ligand |
