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The crystal structure of a secreted protein esxb (wild-type, in P21 space group) from bacillus anthracis str. sterne
Analyse The crystal structure of a secreted protein esxb (wild-type, in P21 space… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4J11
- Type
- protein
- Length
- 357 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Secreted protein esxb
- UniProt
- Q81R67
- Pockets
- 4 · best druggability 0.55
Structure
x-ray diffraction · 4 distinct chains · 82% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Secreted protein esxb | protein | 87 | 83% helix, 0% strand | Q81R67 |
| B | Secreted protein esxb | protein | 93 | 78% helix, 2% strand | Q81R67 |
| C | Secreted protein esxb | protein | 91 | 85% helix, 0% strand | Q81R67 |
| D | Secreted protein esxb | protein | 86 | 84% helix, 0% strand | Q81R67 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 111 | 0.55 | 0.84 | 24 | empty |
| 2 | 180 | 0.51 | 0.77 | 35 | empty |
| 3 | 55 | 0.34 | 0.78 | 17 | empty |
| 4 | 82 | 0.31 | 0.73 | 19 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1748 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1675 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 663 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 271 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 4J11 · The crystal structure of a secreted protein ESXB (wild-type, in P21 space group) from… · the same entry in another collection · chain A 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 Q81R67
- Elsewhere: RCSB PDB 4J11 · PDBe 4J11 · UniProt Q81R67
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