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Crystal structure of ectromelia virus EVM1 chemokine binding protein
Analyse Crystal structure of ectromelia virus EVM1 chemokine binding protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GRK
- Type
- protein
- Length
- 456 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- EVM001
- UniProt
- Q9JFS0
- Pockets
- 7 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | EVM001 | protein | 228 | 8% helix, 44% strand | Q9JFS0 |
Pockets
7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 106 | 0.39 | 0.76 | 23 | empty |
| 2 | 79 | 0.37 | 0.77 | 18 | empty |
| 3 | 84 | 0.37 | 0.76 | 18 | empty |
| 4 | 143 | 0.36 | 0.72 | 23 | empty |
| 5 | 109 | 0.34 | 0.73 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 854 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 2GRK · Crystal structure of ectromelia virus EVM1 chemokine binding protein · 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 Q9JFS0
- Elsewhere: RCSB PDB 2GRK · PDBe 2GRK · UniProt Q9JFS0
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