Research workbench
Tesa a major thioesterase from mycobacterium tuberculosis
Analyse Tesa a major thioesterase 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
- 6FW5
- Type
- protein
- Length
- 888 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P9WQD4
- Ligands
- PO4
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 233 | — | P9WQD4 |
| B | — | protein | 223 | — | P9WQD4 |
| C | — | protein | 208 | — | P9WQD4 |
| D | — | protein | 224 | — | P9WQD4 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 P9WQD4
- Elsewhere: RCSB PDB 6FW5 · PDBe 6FW5 · UniProt P9WQD4
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