2NYP
Structure of beta-lactamase II from Bacillus cereus. R121H, C221D doble mutant with two zinc ions.
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | HIS86 |
| A | HIS88 |
| A | HIS149 |
| A | ASP168 |
| A | HOH417 |
| A | HOH432 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 302 |
| Chain | Residue |
| A | HIS210 |
| A | HOH417 |
| A | HOH463 |
| A | ASP90 |
| A | HIS91 |
| A | ASP168 |
Functional Information from PROSITE/UniProt
| site_id | PS00743 |
| Number of Residues | 20 |
| Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IiTHaHADhiGGiktlker.G |
| Chain | Residue | Details |
| A | ILE83-GLY102 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20677753","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24059435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7588620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761898","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20677753","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24059435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761898","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP90 | |
| A | ASN180 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP90 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 16 |
| Chain | Residue | Details |
| A | HIS86 | metal ligand |
| A | HIS88 | metal ligand |
| A | ASP90 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS149 | metal ligand |
| A | ASN180 | electrostatic stabiliser, hydrogen bond donor |
