4NCR
Crystal structure of M. tuberculosis DprE1 in complex with PBTZ169
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003885 | molecular_function | D-arabinono-1,4-lactone oxidase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0035884 | biological_process | arabinan biosynthetic process |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0045227 | biological_process | capsule polysaccharide biosynthetic process |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0070592 | biological_process | cell wall polysaccharide biosynthetic process |
| A | 0071555 | biological_process | cell wall organization |
| A | 0071949 | molecular_function | FAD binding |
| B | 0003885 | molecular_function | D-arabinono-1,4-lactone oxidase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0035884 | biological_process | arabinan biosynthetic process |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0045227 | biological_process | capsule polysaccharide biosynthetic process |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0070592 | biological_process | cell wall polysaccharide biosynthetic process |
| B | 0071555 | biological_process | cell wall organization |
| B | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 26J A 501 |
| Chain | Residue |
| A | GLY117 |
| A | HOH690 |
| A | GLY133 |
| A | LYS134 |
| A | SER228 |
| A | LYS367 |
| A | ASN385 |
| A | CYS387 |
| A | LYS418 |
| A | FAD502 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD A 502 |
| Chain | Residue |
| A | TRP16 |
| A | ILE52 |
| A | ALA53 |
| A | ARG54 |
| A | GLY55 |
| A | LEU56 |
| A | GLY57 |
| A | ARG58 |
| A | SER59 |
| A | TYR60 |
| A | ASN63 |
| A | ALA64 |
| A | MET74 |
| A | ALA94 |
| A | PRO116 |
| A | GLY117 |
| A | THR118 |
| A | VAL121 |
| A | THR122 |
| A | GLY124 |
| A | GLY125 |
| A | ALA128 |
| A | CYS129 |
| A | ILE131 |
| A | HIS132 |
| A | ASN178 |
| A | GLY179 |
| A | GLY182 |
| A | ILE184 |
| A | TYR415 |
| A | ALA417 |
| A | 26J501 |
| A | HOH629 |
| A | HOH633 |
| A | HOH692 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | TRP230 |
| A | PHE231 |
| A | TYR297 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 504 |
| Chain | Residue |
| A | SER82 |
| A | ASP84 |
| A | THR87 |
| A | LEU89 |
| A | THR188 |
| B | IMD504 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 505 |
| Chain | Residue |
| B | ASP204 |
| B | ASP218 |
| B | ARG223 |
| B | ARG247 |
| B | HOH630 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 26J B 501 |
| Chain | Residue |
| B | GLY117 |
| B | HIS132 |
| B | GLY133 |
| B | LYS134 |
| B | VAL365 |
| B | LYS367 |
| B | ASN385 |
| B | CYS387 |
| B | LYS418 |
| B | FAD502 |
| B | HOH657 |
| site_id | AC7 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD B 502 |
| Chain | Residue |
| B | ALA417 |
| B | 26J501 |
| B | HOH610 |
| B | HOH645 |
| B | TRP16 |
| B | ILE52 |
| B | ALA53 |
| B | ARG54 |
| B | GLY55 |
| B | LEU56 |
| B | GLY57 |
| B | ARG58 |
| B | SER59 |
| B | TYR60 |
| B | ASN63 |
| B | ALA64 |
| B | ALA94 |
| B | PRO116 |
| B | GLY117 |
| B | THR118 |
| B | VAL121 |
| B | THR122 |
| B | GLY124 |
| B | GLY125 |
| B | ALA128 |
| B | CYS129 |
| B | ILE131 |
| B | HIS132 |
| B | ASN178 |
| B | GLY179 |
| B | GLY182 |
| B | ILE184 |
| B | TYR415 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| A | PRO107 |
| A | PHE108 |
| B | ASN78 |
| B | THR79 |
| B | ILE80 |
| B | GLN100 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IMD B 504 |
| Chain | Residue |
| A | SER82 |
| A | ASP84 |
| A | GOL504 |
| B | SER82 |
| B | ASP84 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22733761, ECO:0000269|PubMed:23776209, ECO:0000269|PubMed:24500695, ECO:0000269|PubMed:25427196, ECO:0007744|PDB:4FDP, ECO:0007744|PDB:4NCR |
| Chain | Residue | Details |
| A | ALA53 | |
| B | ALA53 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22733761, ECO:0000269|PubMed:23776209, ECO:0000269|PubMed:24500695, ECO:0000269|PubMed:25427196, ECO:0007744|PDB:4FDP, ECO:0007744|PDB:4KW5, ECO:0007744|PDB:4NCR |
| Chain | Residue | Details |
| A | TYR415 | |
| B | GLY117 | |
| B | THR122 | |
| B | CYS129 | |
| B | ILE184 | |
| B | TYR415 | |
| A | GLY117 | |
| A | THR122 | |
| A | CYS129 | |
| A | ILE184 |
