Research workbench
Crystal structure of cag VIRB11 (HP0525) and an inhibitory protein (HP1451)
Analyse Crystal structure of cag VIRB11 (HP0525) and an inhibitory protein (HP1451) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PT7
- Type
- protein
- Length
- 2,166 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cag-alfa; Hypothetical protein
- UniProt
- Q7BK04, O25990
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Cag-alfa | protein | 323 | 39% helix, 22% strand | Q7BK04 |
| B, E | Cag-alfa | protein | 308 | 35% helix, 23% strand | Q7BK04 |
| C, F | Cag-alfa | protein | 307 | 35% helix, 23% strand | Q7BK04 |
| G, H | Hypothetical protein | protein | 145 | 48% helix, 26% strand | O25990 |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1115 | 0.85 | 0.87 | 118 | empty |
| 2 | 787 | 0.85 | 0.88 | 92 | empty |
| 3 | 976 | 0.84 | 0.85 | 107 | empty |
| 4 | 998 | 0.84 | 0.85 | 103 | empty |
| 5 | 1106 | 0.82 | 0.83 | 107 | empty |
Interfaces
16 interfaces between chains.
- A–B · 1803 Ų buried · 29 hydrogen bonds · protein-protein
- D–E · 1774 Ų buried · 31 hydrogen bonds · protein-protein
- A–F · 1700 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 1685 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 1649 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 2PT7 · Crystal structure of Cag VirB11 (HP0525) and an inhibitory protein (HP1451) · 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 Q7BK04
- Every structure of UniProt O25990
- Elsewhere: RCSB PDB 2PT7 · PDBe 2PT7 · UniProt Q7BK04 · UniProt O25990
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