MolNFT v1 · #183841 · protein
Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme with coenzyme a bound at the hydratase, thiolase active sites and additional binding site (COA(ECH2))
7O4S: “Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme with coenzyme a bound at the…”. X-ray diffraction, 4 ligands (COA, PAP, ADP). MolNFT v1 #183841 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 7O4S
- Type
- protein
- Length
- 2,261 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O53872, O53871
- Ligands
- COA, PAP, ADP, SO4
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 729 | — | O53872 |
| B | — | protein | 728 | — | O53872 |
| C, D | — | protein | 402 | — | O53871 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 6 copies · chains A, B, C, D
- PAP · 3'-phosphate-adenosine-5'-diphosphate · ligand · chains B, C
- ADP · Adenosine-5'-diphosphate · ligand · chains A, D
- SO4 · Sulfate ion · ion · 26 copies · chains A, C, D, B
- GOL · Glycerol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7O4S · Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme with Coenzyme… · the same entry in another collection · chain A against A, TM-score 1.00
- O53871 · AlphaFold monomer V2.0 prediction for putative acyltransferase RV0859 (O53871) · a predicted model of the same protein · chain C against A, TM-score 1.00
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 O53872
- Every structure of UniProt O53871
- Elsewhere: RCSB PDB 7O4S · PDBe 7O4S · UniProt O53872 · UniProt O53871
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