5MTR
Crystal structure of M. tuberculosis InhA inhibited by PT512
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
A | 0005504 | molecular_function | fatty acid binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0009274 | cellular_component | peptidoglycan-based cell wall |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0030497 | biological_process | fatty acid elongation |
A | 0046677 | biological_process | response to antibiotic |
A | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
A | 0070403 | molecular_function | NAD+ binding |
A | 0071768 | biological_process | mycolic acid biosynthetic process |
B | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
B | 0005504 | molecular_function | fatty acid binding |
B | 0005886 | cellular_component | plasma membrane |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0009274 | cellular_component | peptidoglycan-based cell wall |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0030497 | biological_process | fatty acid elongation |
B | 0046677 | biological_process | response to antibiotic |
B | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
B | 0070403 | molecular_function | NAD+ binding |
B | 0071768 | biological_process | mycolic acid biosynthetic process |
C | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
C | 0005504 | molecular_function | fatty acid binding |
C | 0005886 | cellular_component | plasma membrane |
C | 0006633 | biological_process | fatty acid biosynthetic process |
C | 0009274 | cellular_component | peptidoglycan-based cell wall |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0030497 | biological_process | fatty acid elongation |
C | 0046677 | biological_process | response to antibiotic |
C | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
C | 0070403 | molecular_function | NAD+ binding |
C | 0071768 | biological_process | mycolic acid biosynthetic process |
D | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
D | 0005504 | molecular_function | fatty acid binding |
D | 0005886 | cellular_component | plasma membrane |
D | 0006633 | biological_process | fatty acid biosynthetic process |
D | 0009274 | cellular_component | peptidoglycan-based cell wall |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0030497 | biological_process | fatty acid elongation |
D | 0046677 | biological_process | response to antibiotic |
D | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
D | 0070403 | molecular_function | NAD+ binding |
D | 0071768 | biological_process | mycolic acid biosynthetic process |
E | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
E | 0005504 | molecular_function | fatty acid binding |
E | 0005886 | cellular_component | plasma membrane |
E | 0006633 | biological_process | fatty acid biosynthetic process |
E | 0009274 | cellular_component | peptidoglycan-based cell wall |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0030497 | biological_process | fatty acid elongation |
E | 0046677 | biological_process | response to antibiotic |
E | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
E | 0070403 | molecular_function | NAD+ binding |
E | 0071768 | biological_process | mycolic acid biosynthetic process |
F | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
F | 0005504 | molecular_function | fatty acid binding |
F | 0005886 | cellular_component | plasma membrane |
F | 0006633 | biological_process | fatty acid biosynthetic process |
F | 0009274 | cellular_component | peptidoglycan-based cell wall |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0030497 | biological_process | fatty acid elongation |
F | 0046677 | biological_process | response to antibiotic |
F | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
F | 0070403 | molecular_function | NAD+ binding |
F | 0071768 | biological_process | mycolic acid biosynthetic process |
G | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
G | 0005504 | molecular_function | fatty acid binding |
G | 0005886 | cellular_component | plasma membrane |
G | 0006633 | biological_process | fatty acid biosynthetic process |
G | 0009274 | cellular_component | peptidoglycan-based cell wall |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0030497 | biological_process | fatty acid elongation |
G | 0046677 | biological_process | response to antibiotic |
G | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
G | 0070403 | molecular_function | NAD+ binding |
G | 0071768 | biological_process | mycolic acid biosynthetic process |
H | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
H | 0005504 | molecular_function | fatty acid binding |
H | 0005886 | cellular_component | plasma membrane |
H | 0006633 | biological_process | fatty acid biosynthetic process |
H | 0009274 | cellular_component | peptidoglycan-based cell wall |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0030497 | biological_process | fatty acid elongation |
H | 0046677 | biological_process | response to antibiotic |
H | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
H | 0070403 | molecular_function | NAD+ binding |
H | 0071768 | biological_process | mycolic acid biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 33 |
Details | binding site for residue NAD A 301 |
Chain | Residue |
A | GLY14 |
A | SER94 |
A | ILE95 |
A | GLY96 |
A | ILE122 |
A | MET147 |
A | ASP148 |
A | PHE149 |
A | LYS165 |
A | ALA191 |
A | GLY192 |
A | ILE15 |
A | PRO193 |
A | ILE194 |
A | THR196 |
A | ALA198 |
A | XT0302 |
A | HOH418 |
A | HOH423 |
A | HOH427 |
A | HOH443 |
A | HOH469 |
A | ILE16 |
A | HOH476 |
A | HOH489 |
A | HOH495 |
A | HOH505 |
A | SER20 |
A | ILE21 |
A | PHE41 |
A | LEU63 |
A | ASP64 |
A | VAL65 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue XT0 A 302 |
Chain | Residue |
A | GLY96 |
A | PHE97 |
A | MET98 |
A | MET103 |
A | PRO156 |
A | TYR158 |
A | LYS165 |
A | ALA198 |
A | MET199 |
A | VAL203 |
A | GLN214 |
A | LEU218 |
A | NAD301 |
site_id | AC3 |
Number of Residues | 32 |
Details | binding site for residue NAD B 301 |
Chain | Residue |
B | GLY14 |
B | ILE15 |
B | ILE16 |
B | SER20 |
B | ILE21 |
B | PHE41 |
B | LEU63 |
B | ASP64 |
B | VAL65 |
B | SER94 |
B | ILE95 |
B | GLY96 |
B | ILE122 |
B | MET147 |
B | ASP148 |
B | LYS165 |
B | ALA191 |
B | GLY192 |
B | PRO193 |
B | ILE194 |
B | THR196 |
B | LEU197 |
B | ALA198 |
B | XT0302 |
B | HOH415 |
B | HOH418 |
B | HOH425 |
B | HOH440 |
B | HOH456 |
B | HOH463 |
B | HOH507 |
B | HOH509 |
site_id | AC4 |
Number of Residues | 16 |
Details | binding site for residue XT0 B 302 |
Chain | Residue |
B | GLY96 |
B | PHE97 |
B | MET103 |
B | PHE149 |
B | MET155 |
B | PRO156 |
B | ALA157 |
B | TYR158 |
B | MET161 |
B | LYS165 |
B | ALA198 |
B | MET199 |
B | ILE202 |
B | GLN214 |
B | LEU218 |
B | NAD301 |
site_id | AC5 |
Number of Residues | 32 |
Details | binding site for residue NAD E 301 |
Chain | Residue |
E | PHE41 |
E | LEU63 |
E | ASP64 |
E | VAL65 |
E | SER94 |
E | ILE95 |
E | GLY96 |
E | ILE122 |
E | MET147 |
E | ASP148 |
E | PHE149 |
E | LYS165 |
E | ALA191 |
E | GLY192 |
E | PRO193 |
E | ILE194 |
E | THR196 |
E | ALA198 |
E | XT0302 |
E | HOH415 |
E | HOH419 |
E | HOH448 |
E | HOH453 |
E | HOH463 |
E | HOH490 |
E | HOH497 |
E | HOH502 |
E | GLY14 |
E | ILE15 |
E | ILE16 |
E | SER20 |
E | ILE21 |
site_id | AC6 |
Number of Residues | 14 |
Details | binding site for residue XT0 E 302 |
Chain | Residue |
E | GLY96 |
E | PHE97 |
E | MET103 |
E | PHE149 |
E | MET155 |
E | PRO156 |
E | TYR158 |
E | MET161 |
E | ALA198 |
E | MET199 |
E | ILE202 |
E | GLN214 |
E | LEU218 |
E | NAD301 |
site_id | AC7 |
Number of Residues | 31 |
Details | binding site for residue NAD G 301 |
Chain | Residue |
G | GLY14 |
G | ILE15 |
G | ILE16 |
G | SER20 |
G | ILE21 |
G | PHE41 |
G | LEU63 |
G | ASP64 |
G | VAL65 |
G | SER94 |
G | ILE95 |
G | GLY96 |
G | ILE122 |
G | MET147 |
G | ASP148 |
G | PHE149 |
G | LYS165 |
G | ALA191 |
G | GLY192 |
G | PRO193 |
G | ILE194 |
G | THR196 |
G | LEU197 |
G | ALA198 |
G | XT0302 |
G | HOH424 |
G | HOH427 |
G | HOH436 |
G | HOH460 |
G | HOH472 |
G | HOH476 |
site_id | AC8 |
Number of Residues | 14 |
Details | binding site for residue XT0 G 302 |
Chain | Residue |
G | GLY96 |
G | PHE97 |
G | MET103 |
G | PHE149 |
G | MET155 |
G | PRO156 |
G | TYR158 |
G | MET161 |
G | ALA198 |
G | MET199 |
G | ILE202 |
G | GLN214 |
G | LEU218 |
G | NAD301 |
site_id | AC9 |
Number of Residues | 34 |
Details | binding site for residue NAD C 301 |
Chain | Residue |
C | GLY14 |
C | ILE15 |
C | ILE16 |
C | SER20 |
C | ILE21 |
C | PHE41 |
C | LEU63 |
C | ASP64 |
C | VAL65 |
C | SER94 |
C | ILE95 |
C | GLY96 |
C | ILE122 |
C | MET147 |
C | ASP148 |
C | PHE149 |
C | LYS165 |
C | ALA191 |
C | GLY192 |
C | PRO193 |
C | ILE194 |
C | THR196 |
C | LEU197 |
C | ALA198 |
C | XT0302 |
C | HOH404 |
C | HOH415 |
C | HOH443 |
C | HOH449 |
C | HOH455 |
C | HOH475 |
C | HOH478 |
C | HOH505 |
C | HOH508 |
site_id | AD1 |
Number of Residues | 14 |
Details | binding site for residue XT0 C 302 |
Chain | Residue |
C | GLY96 |
C | PHE97 |
C | MET103 |
C | PHE149 |
C | MET155 |
C | PRO156 |
C | TYR158 |
C | MET161 |
C | ALA198 |
C | MET199 |
C | ILE202 |
C | VAL203 |
C | GLN214 |
C | NAD301 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue CL C 303 |
Chain | Residue |
C | PRO237 |
C | HOH427 |
site_id | AD3 |
Number of Residues | 30 |
Details | binding site for residue NAD D 301 |
Chain | Residue |
D | GLY14 |
D | ILE15 |
D | ILE16 |
D | SER20 |
D | ILE21 |
D | PHE41 |
D | LEU63 |
D | ASP64 |
D | VAL65 |
D | SER94 |
D | ILE95 |
D | GLY96 |
D | ILE122 |
D | MET147 |
D | ASP148 |
D | PHE149 |
D | LYS165 |
D | ALA191 |
D | GLY192 |
D | PRO193 |
D | ILE194 |
D | THR196 |
D | ALA198 |
D | XT0302 |
D | HOH404 |
D | HOH412 |
D | HOH432 |
D | HOH440 |
D | HOH442 |
D | HOH463 |
site_id | AD4 |
Number of Residues | 13 |
Details | binding site for residue XT0 D 302 |
Chain | Residue |
D | GLY96 |
D | PHE97 |
D | MET103 |
D | PHE149 |
D | MET155 |
D | PRO156 |
D | TYR158 |
D | MET161 |
D | ALA198 |
D | MET199 |
D | ILE202 |
D | GLN214 |
D | NAD301 |
site_id | AD5 |
Number of Residues | 31 |
Details | binding site for residue NAD F 301 |
Chain | Residue |
F | GLY14 |
F | ILE15 |
F | ILE16 |
F | SER20 |
F | ILE21 |
F | PHE41 |
F | LEU63 |
F | ASP64 |
F | VAL65 |
F | SER94 |
F | ILE95 |
F | GLY96 |
F | ILE122 |
F | MET147 |
F | ASP148 |
F | PHE149 |
F | LYS165 |
F | ALA191 |
F | GLY192 |
F | PRO193 |
F | ILE194 |
F | THR196 |
F | ALA198 |
F | XT0302 |
F | HOH426 |
F | HOH458 |
F | HOH467 |
F | HOH468 |
F | HOH473 |
F | HOH501 |
F | HOH502 |
site_id | AD6 |
Number of Residues | 14 |
Details | binding site for residue XT0 F 302 |
Chain | Residue |
F | GLY96 |
F | PHE97 |
F | MET98 |
F | PHE149 |
F | MET155 |
F | PRO156 |
F | TYR158 |
F | MET161 |
F | ALA198 |
F | MET199 |
F | GLN214 |
F | LEU217 |
F | LEU218 |
F | NAD301 |
site_id | AD7 |
Number of Residues | 31 |
Details | binding site for residue NAD H 301 |
Chain | Residue |
H | GLY14 |
H | ILE15 |
H | ILE16 |
H | SER20 |
H | ILE21 |
H | PHE41 |
H | LEU63 |
H | ASP64 |
H | VAL65 |
H | SER94 |
H | ILE95 |
H | GLY96 |
H | ILE122 |
H | MET147 |
H | ASP148 |
H | PHE149 |
H | LYS165 |
H | ALA191 |
H | GLY192 |
H | PRO193 |
H | ILE194 |
H | THR196 |
H | LEU197 |
H | ALA198 |
H | XT0302 |
H | HOH405 |
H | HOH423 |
H | HOH431 |
H | HOH438 |
H | HOH471 |
H | HOH475 |
site_id | AD8 |
Number of Residues | 14 |
Details | binding site for residue XT0 H 302 |
Chain | Residue |
H | GLY96 |
H | PHE97 |
H | MET103 |
H | PHE149 |
H | MET155 |
H | PRO156 |
H | TYR158 |
H | MET161 |
H | ALA198 |
H | MET199 |
H | ILE202 |
H | GLN214 |
H | LEU218 |
H | NAD301 |
site_id | AD9 |
Number of Residues | 3 |
Details | binding site for residue CL H 303 |
Chain | Residue |
H | LEU61 |
H | GLU62 |
H | ARG77 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 |
Chain | Residue | Details |
A | SER20 | |
B | ILE194 | |
E | SER20 | |
E | ASP64 | |
E | ILE95 | |
E | LYS165 | |
E | ILE194 | |
G | SER20 | |
G | ASP64 | |
G | ILE95 | |
G | LYS165 | |
A | ASP64 | |
G | ILE194 | |
C | SER20 | |
C | ASP64 | |
C | ILE95 | |
C | LYS165 | |
C | ILE194 | |
D | SER20 | |
D | ASP64 | |
D | ILE95 | |
D | LYS165 | |
A | ILE95 | |
D | ILE194 | |
F | SER20 | |
F | ASP64 | |
F | ILE95 | |
F | LYS165 | |
F | ILE194 | |
H | SER20 | |
H | ASP64 | |
H | ILE95 | |
H | LYS165 | |
A | LYS165 | |
H | ILE194 | |
A | ILE194 | |
B | SER20 | |
B | ASP64 | |
B | ILE95 | |
B | LYS165 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10336454 |
Chain | Residue | Details |
A | TYR158 | |
B | TYR158 | |
E | TYR158 | |
G | TYR158 | |
C | TYR158 | |
D | TYR158 | |
F | TYR158 | |
H | TYR158 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: May act as an intermediate that passes the hydride ion from NADH to the substrate => ECO:0000305|PubMed:10336454 |
Chain | Residue | Details |
A | PHE149 | |
B | PHE149 | |
E | PHE149 | |
G | PHE149 | |
C | PHE149 | |
D | PHE149 | |
F | PHE149 | |
H | PHE149 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:10521269 |
Chain | Residue | Details |
A | TYR158 | |
B | TYR158 | |
E | TYR158 | |
G | TYR158 | |
C | TYR158 | |
D | TYR158 | |
F | TYR158 | |
H | TYR158 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:20864541, ECO:0000269|PubMed:21143326 |
Chain | Residue | Details |
A | THR266 | |
B | THR266 | |
E | THR266 | |
G | THR266 | |
C | THR266 | |
D | THR266 | |
F | THR266 | |
H | THR266 |