1R44
Crystal Structure of VanX
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016805 | molecular_function | dipeptidase activity |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071555 | biological_process | cell wall organization |
| A | 0160237 | molecular_function | D-Ala-D-Ala dipeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016805 | molecular_function | dipeptidase activity |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
| B | 0160237 | molecular_function | D-Ala-D-Ala dipeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008233 | molecular_function | peptidase activity |
| C | 0008237 | molecular_function | metallopeptidase activity |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016805 | molecular_function | dipeptidase activity |
| C | 0046677 | biological_process | response to antibiotic |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0071555 | biological_process | cell wall organization |
| C | 0160237 | molecular_function | D-Ala-D-Ala dipeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008233 | molecular_function | peptidase activity |
| D | 0008237 | molecular_function | metallopeptidase activity |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016805 | molecular_function | dipeptidase activity |
| D | 0046677 | biological_process | response to antibiotic |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0071555 | biological_process | cell wall organization |
| D | 0160237 | molecular_function | D-Ala-D-Ala dipeptidase activity |
| E | 0006508 | biological_process | proteolysis |
| E | 0008233 | molecular_function | peptidase activity |
| E | 0008237 | molecular_function | metallopeptidase activity |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0016805 | molecular_function | dipeptidase activity |
| E | 0046677 | biological_process | response to antibiotic |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0071555 | biological_process | cell wall organization |
| E | 0160237 | molecular_function | D-Ala-D-Ala dipeptidase activity |
| F | 0006508 | biological_process | proteolysis |
| F | 0008233 | molecular_function | peptidase activity |
| F | 0008237 | molecular_function | metallopeptidase activity |
| F | 0008270 | molecular_function | zinc ion binding |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0016805 | molecular_function | dipeptidase activity |
| F | 0046677 | biological_process | response to antibiotic |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0071555 | biological_process | cell wall organization |
| F | 0160237 | molecular_function | D-Ala-D-Ala dipeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 203 |
| Chain | Residue |
| A | HIS116 |
| A | ASP123 |
| A | HIS184 |
| A | HOH205 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 203 |
| Chain | Residue |
| B | HIS116 |
| B | ASP123 |
| B | HIS184 |
| B | HOH204 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN C 203 |
| Chain | Residue |
| C | ASP123 |
| C | HIS184 |
| C | HIS116 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 203 |
| Chain | Residue |
| D | HIS116 |
| D | ASP123 |
| D | HIS184 |
| D | HOH204 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 203 |
| Chain | Residue |
| E | HIS116 |
| E | ASP123 |
| E | HIS184 |
| E | HOH205 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 203 |
| Chain | Residue |
| F | HIS116 |
| F | ASP123 |
| F | HIS184 |
| F | HOH205 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"9702193","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01924","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9702193","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| A | GLU181 | |
| A | ARG71 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| B | GLU181 | |
| B | ARG71 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| C | GLU181 | |
| C | ARG71 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| D | GLU181 | |
| D | ARG71 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| E | GLU181 | |
| E | ARG71 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| F | GLU181 | |
| F | ARG71 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 706 |
| Chain | Residue | Details |
| A | ARG71 | electrostatic stabiliser |
| A | HIS116 | metal ligand |
| A | ASP123 | metal ligand |
| A | GLU181 | proton acceptor, proton donor |
| A | HIS184 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 706 |
| Chain | Residue | Details |
| B | ARG71 | electrostatic stabiliser |
| B | HIS116 | metal ligand |
| B | ASP123 | metal ligand |
| B | GLU181 | proton acceptor, proton donor |
| B | HIS184 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 706 |
| Chain | Residue | Details |
| C | ARG71 | electrostatic stabiliser |
| C | HIS116 | metal ligand |
| C | ASP123 | metal ligand |
| C | GLU181 | proton acceptor, proton donor |
| C | HIS184 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 706 |
| Chain | Residue | Details |
| D | ARG71 | electrostatic stabiliser |
| D | HIS116 | metal ligand |
| D | ASP123 | metal ligand |
| D | GLU181 | proton acceptor, proton donor |
| D | HIS184 | metal ligand |
| site_id | MCSA5 |
| Number of Residues | 5 |
| Details | M-CSA 706 |
| Chain | Residue | Details |
| E | ARG71 | electrostatic stabiliser |
| E | HIS116 | metal ligand |
| E | ASP123 | metal ligand |
| E | GLU181 | proton acceptor, proton donor |
| E | HIS184 | metal ligand |
| site_id | MCSA6 |
| Number of Residues | 5 |
| Details | M-CSA 706 |
| Chain | Residue | Details |
| F | ARG71 | electrostatic stabiliser |
| F | HIS116 | metal ligand |
| F | ASP123 | metal ligand |
| F | GLU181 | proton acceptor, proton donor |
| F | HIS184 | metal ligand |
