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Crystal structure of a putative uncharacterized protein from burkholderia thailandensis
Analyse Crystal structure of a putative uncharacterized protein from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AR7
- Type
- protein
- Length
- 821 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q2T081
- Pockets
- 5 · best druggability 0.88
Structure
x-ray diffraction · 4 distinct chains · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 205 | 81% helix, 0% strand | Q2T081 |
| B | Uncharacterized protein | protein | 206 | 82% helix, 0% strand | Q2T081 |
| C | Uncharacterized protein | protein | 207 | 82% helix, 0% strand | Q2T081 |
| D | Uncharacterized protein | protein | 203 | 82% helix, 0% strand | Q2T081 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1086 | 0.88 | 0.89 | 107 | empty |
| 2 | 1028 | 0.87 | 0.88 | 106 | empty |
| 3 | 1087 | 0.76 | 0.78 | 76 | empty |
| 4 | 51 | 0.28 | 0.74 | 10 | empty |
| 5 | 60 | 0.27 | 0.73 | 14 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1401 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 1389 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 295 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 40 modified, 8 disulfide (engineered, disulfide).
Compared structures
- 6AR7 · Crystal structure of a putative uncharacterized protein from Burkholderia thailandensis · 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 Q2T081
- Elsewhere: RCSB PDB 6AR7 · PDBe 6AR7 · UniProt Q2T081
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