MolNFT v2 · #165450 · protein
Crystal structure of M. tuberculosis InhA in complex with NAD+ and 3-[3-(trifluoromethyl)phenyl]prop-2-enoic acid
6SQ5: “Crystal structure of M. tuberculosis InhA in complex with NAD+ and 3-[3-(trifluoromethyl)phenyl]prop-2-enoic…”. X-ray diffraction at 1.84, 2 ligands (NAD, LRW). MolNFT v2 #165450 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6SQ5
- Type
- protein
- Length
- 267 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.84
- Source
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- UniProt
- P9WGR1
- Ligands
- NAD, LRW
Structure
x-ray diffraction · resolution 1.84 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 267 | — | P9WGR1 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
- LRW · (~{E})-3-[3-(trifluoromethyl)phenyl]prop-2-enoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6SQ5 · Crystal structure of M. tuberculosis inha in complex with NAD+ and 3… · the same entry in another collection · chain A against A, TM-score 1.00
- P9WGR1 · AlphaFold monomer V2.0 prediction for enoyl-[acyl-carrier-protein] reductase [NADH]… · a predicted model of the same protein · chain A against A, TM-score 0.96
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P9WGR1
- Elsewhere: RCSB PDB 6SQ5 · PDBe 6SQ5 · UniProt P9WGR1
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