3BZM
Crystal Structure of Open form of Menaquinone-Specific Isochorismate Synthase, MenF
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CIT A 432 |
Chain | Residue |
A | GLN57 |
A | ARG58 |
A | ASN59 |
A | ARG241 |
A | ARG244 |
A | ARG251 |
A | HOH520 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01935, ECO:0000269|PubMed:17240978 |
Chain | Residue | Details |
A | LYS190 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01935, ECO:0000269|PubMed:17240978 |
Chain | Residue | Details |
A | GLU240 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01935, ECO:0000269|PubMed:18453696 |
Chain | Residue | Details |
A | GLU284 | |
A | GLU416 |
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 | 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 |