Research workbench
Negative stain EM reconstruction of M.TUBERCULOSIS ACR1(HSP 16.3) fitted with wheat shsp dimer
Analyse Negative stain EM reconstruction of M.TUBERCULOSIS ACR1(HSP 16.3) fitted with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BYU
- Type
- protein
- Length
- 1,212 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein 16.9B
- UniProt
- Q41560
- Pockets
- 20 · best druggability 0.62
Structure
electron microscopy · 1 distinct chain · 6% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Heat shock protein 16.9B | protein | 101 | 6% helix, 49% strand | Q41560 |
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 170 | 0.62 | 0.84 | 31 | empty |
| 2 | 167 | 0.61 | 0.84 | 31 | empty |
| 3 | 174 | 0.61 | 0.83 | 31 | empty |
| 4 | 169 | 0.61 | 0.83 | 31 | empty |
| 5 | 168 | 0.61 | 0.83 | 26 | empty |
Interfaces
24 interfaces between chains.
- G–H · 1563 Ų buried · 37 hydrogen bonds · protein-protein
- I–J · 1562 Ų buried · 37 hydrogen bonds · protein-protein
- C–D · 1561 Ų buried · 37 hydrogen bonds · protein-protein
- A–B · 1560 Ų buried · 37 hydrogen bonds · protein-protein
- K–L · 1559 Ų buried · 37 hydrogen bonds · protein-protein
Compared structures
- 2BYU · Negative stain EM reconstruction of M.tuberculosis Acr1(Hsp 16.3) fitted with wheat sHSP… · the same entry in another collection · chain L against L, 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 Q41560
- Elsewhere: RCSB PDB 2BYU · PDBe 2BYU · UniProt Q41560
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