MolNFT v1 · #106242 · protein
Crystal structure of molecular chaperone dnak from mycobacterium tuberculosis H37RV
4RTF · Chaperone protein dnak: “Crystal structure of molecular chaperone dnak from mycobacterium tuberculosis H37RV”. X-ray diffraction, 1 ligand (ATP), 2 pockets (best druggability 0.71). MolNFT v1 #106242 on GenesisL1: 3D structure…
- PDB
- 4RTF
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein dnak
- UniProt
- I6Y7L1
- Ligands
- ATP
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | Chaperone protein dnak | protein | 349 | 41% helix, 28% strand | I6Y7L1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 521 | 0.71 | 0.80 | 62 | ATP |
| 2 | 61 | 0.32 | 0.76 | 16 | empty |
Compared structures
- 4RTF · Crystal structure of molecular chaperone DnaK from Mycobacterium tuberculosis H37Rv · the same entry in another collection · chain D against D, 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 I6Y7L1
- Elsewhere: RCSB PDB 4RTF · PDBe 4RTF · UniProt I6Y7L1
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