1RJM
Crystal Structure of MenB (Rv0548c) from Mycobacterium tuberculosis
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 | 27 |
| Details | BINDING SITE FOR RESIDUE EP1 A 315 |
| Chain | Residue |
| A | ARG202 |
| A | HOH327 |
| A | HOH375 |
| A | HOH376 |
| A | HOH377 |
| B | ALA201 |
| B | ARG202 |
| B | GLN203 |
| B | VAL204 |
| B | GLY205 |
| B | GLN226 |
| A | GLN203 |
| B | MET227 |
| C | ARG202 |
| C | GLN203 |
| C | VAL204 |
| C | GLY205 |
| C | PHE208 |
| C | GLN226 |
| C | MET227 |
| A | VAL204 |
| A | GLY205 |
| A | PHE208 |
| A | GLN226 |
| A | MET227 |
| A | HOH324 |
| A | HOH325 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628, ECO:0000269|PubMed:21830810 |
| Chain | Residue | Details |
| A | ARG58 | |
| B | ARG58 | |
| C | ARG58 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:12909628, ECO:0000269|PubMed:21830810 |
| Chain | Residue | Details |
| A | LYS95 | |
| B | LYS95 | |
| C | LYS95 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628, ECO:0000269|PubMed:16131752, ECO:0000269|PubMed:21830810 |
| Chain | Residue | Details |
| A | SER103 | |
| B | SER103 | |
| C | SER103 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: in other chain => ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-Rule:MF_01934 |
| Chain | Residue | Details |
| A | TYR115 | |
| B | TYR115 | |
| C | TYR115 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628 |
| Chain | Residue | Details |
| B | THR184 | |
| C | TRP157 | |
| C | THR184 | |
| A | TRP157 | |
| A | THR184 | |
| B | TRP157 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000305|PubMed:21830810 |
| Chain | Residue | Details |
| A | SER190 | |
| B | SER190 | |
| C | SER190 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-Rule:MF_01934 |
| Chain | Residue | Details |
| B | LYS302 | |
| C | TYR287 | |
| C | LYS302 | |
| A | TYR287 | |
| A | LYS302 | |
| B | TYR287 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | SITE: Important for catalysis => ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-Rule:MF_01934 |
| Chain | Residue | Details |
| A | TYR115 | |
| B | TYR115 | |
| C | TYR115 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | SITE: Important for catalysis => ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000305|PubMed:20643650, ECO:0000305|PubMed:21830810 |
| Chain | Residue | Details |
| A | ASP185 | |
| B | ASP185 | |
| C | ASP185 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | SITE: Important for catalysis => ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000305|PubMed:12909628 |
| Chain | Residue | Details |
| A | TYR287 | |
| B | TYR287 | |
| C | TYR287 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 346 |
| Chain | Residue | Details |
| A | GLY105 | electrostatic stabiliser, hydrogen bond donor |
| A | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
| 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 | 6 |
| Details | M-CSA 346 |
| Chain | Residue | Details |
| B | GLY105 | electrostatic stabiliser, hydrogen bond donor |
| B | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
| 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 | 6 |
| Details | M-CSA 346 |
| Chain | Residue | Details |
| C | GLY105 | electrostatic stabiliser, hydrogen bond donor |
| C | TYR115 | electrostatic stabiliser, hydrogen bond donor, steric role |
| 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 |
