3T8A
Crystal structure of Mycobacterium tuberculosis MenB in complex with substrate analogue, OSB-NCoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
| A | 0009234 | biological_process | menaquinone biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0034214 | biological_process | protein hexamerization |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
| B | 0009234 | biological_process | menaquinone biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0034214 | biological_process | protein hexamerization |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
| C | 0009234 | biological_process | menaquinone biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0034214 | biological_process | protein hexamerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE S0N B 500 |
| Chain | Residue |
| B | VAL57 |
| B | PHE299 |
| B | ARG58 |
| B | ALA60 |
| B | LYS95 |
| B | SER103 |
| B | GLY105 |
| B | ASP106 |
| B | GLN107 |
| B | TRP157 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE S0N C 600 |
| Chain | Residue |
| C | VAL57 |
| C | ARG58 |
| C | SER103 |
| C | GLY105 |
| C | ASP106 |
| C | GLN107 |
| C | TRP157 |
| C | ALA159 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12909628","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"12909628","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12909628","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0ABU0","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Site: {"description":"Important for catalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20643650","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Site: {"description":"Important for catalysis","evidences":[{"source":"UniProtKB","id":"P0ABU0","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12909628","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12909628","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16131752","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 346 |
| Chain | Residue | Details |
| A | GLY105 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY161 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP185 | activator |
| A | SER190 | activator |
| A | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 346 |
| Chain | Residue | Details |
| B | GLY105 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY161 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP185 | activator |
| B | SER190 | activator |
| B | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 346 |
| Chain | Residue | Details |
| C | GLY105 | electrostatic stabiliser, hydrogen bond donor |
| C | GLY161 | electrostatic stabiliser, hydrogen bond donor |
| C | ASP185 | activator |
| C | SER190 | activator |
| C | TYR287 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, steric role |
