2EUA
Structure and Mechanism of MenF, the Menaquinone-Specific Isochorismate Synthase from Escherichia Coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0008909 | molecular_function | isochorismate synthase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009234 | biological_process | menaquinone biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0008909 | molecular_function | isochorismate synthase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009234 | biological_process | menaquinone biosynthetic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TAR A 1000 |
| Chain | Residue |
| A | ARG58 |
| A | ASN59 |
| A | ARG241 |
| A | ARG244 |
| A | ARG251 |
| A | HOH1035 |
| A | HOH1049 |
| A | HOH1066 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TAR B 1001 |
| Chain | Residue |
| B | ASN59 |
| B | ARG241 |
| B | ARG244 |
| B | ARG251 |
| B | HOH1003 |
| B | HOH1056 |
| B | ARG58 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01935","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17240978","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01935","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17240978","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01935","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18453696","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1i7q |
| Chain | Residue | Details |
| A | HIS318 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1i7q |
| Chain | Residue | Details |
| B | HIS318 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 325 |
| Chain | Residue | Details |
| A | LYS190 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU240 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU284 | attractive charge-charge interaction, electrostatic stabiliser, metal ligand |
| A | GLU416 | attractive charge-charge interaction, electrostatic stabiliser, metal ligand |
| A | LYS420 | attractive charge-charge interaction, electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 325 |
| Chain | Residue | Details |
| B | LYS190 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU240 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU284 | attractive charge-charge interaction, electrostatic stabiliser, metal ligand |
| B | GLU416 | attractive charge-charge interaction, electrostatic stabiliser, metal ligand |
| B | LYS420 | attractive charge-charge interaction, electrostatic stabiliser |
