Research workbench
Crystal structure of D175A mutant of RV3272 from mycobacterium tuberculosis
Analyse Crystal structure of D175A mutant of RV3272 from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YIY
- Type
- protein
- Length
- 725 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CoA transferase
- UniProt
- P96877
- Ligands
- CL
- Pockets
- 8 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CoA transferase | protein | 364 | 38% helix, 15% strand | P96877 |
| B | CoA transferase | protein | 361 | 39% helix, 15% strand | P96877 |
Ligands and binding sites
- CL · Chloride ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 847 | 0.77 | 0.80 | 88 | empty |
| 2 | 732 | 0.76 | 0.80 | 73 | empty |
| 3 | 55 | 0.72 | 0.99 | 25 | empty |
| 4 | 90 | 0.38 | 0.76 | 15 | empty |
| 5 | 59 | 0.36 | 0.78 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 6148 Ų buried · 83 hydrogen bonds · protein-protein
Compared structures
- 5YIY · Crystal structure of D175A mutant of Rv3272 from Mycobacterium tuberculosis · the same entry in another collection · chain A against A, TM-score 1.00
- P96877 · AlphaFold monomer V2.0 prediction for probable fatty acyl-CoA transferase RV3272 (P96877) · a predicted model of the same protein · chain B 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 P96877
- Elsewhere: RCSB PDB 5YIY · PDBe 5YIY · UniProt P96877
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