3FCZ
Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility
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 | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 292 |
| Chain | Residue |
| A | HIS116 |
| A | HIS118 |
| A | ASP120 |
| A | HIS196 |
| A | ZN293 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 293 |
| Chain | Residue |
| A | ASP120 |
| A | CYS221 |
| A | HIS263 |
| A | ZN292 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 292 |
| Chain | Residue |
| B | HIS116 |
| B | HIS118 |
| B | ASP120 |
| B | HIS196 |
| B | ZN293 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 293 |
| Chain | Residue |
| B | HOH11 |
| B | ASP120 |
| B | CYS221 |
| B | HIS263 |
| B | ZN292 |
| B | HOH299 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| 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 | 6 |
| 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 | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| 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 | ASP120 | |
| A | ASN233 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP120 | |
| B | ASN233 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP120 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP120 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 16 |
| Chain | Residue | Details |
| A | HIS116 | metal ligand |
| A | HIS118 | metal ligand |
| A | ASP120 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS196 | metal ligand |
| A | ASN233 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 16 |
| Chain | Residue | Details |
| B | HIS116 | metal ligand |
| B | HIS118 | metal ligand |
| B | ASP120 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS196 | metal ligand |
| B | ASN233 | electrostatic stabiliser, hydrogen bond donor |
