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A structural motif in the variant surface glycoproteins of trypanosoma brucei
Analyse A structural motif in the variant surface glycoproteins of trypanosoma brucei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VSG
- Type
- protein
- Length
- 716 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Variant surface glycoprotein iltat 1.24
- UniProt
- P26329
- Pockets
- 7 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Variant surface glycoprotein iltat 1.24 | protein | 358 | 51% helix, 7% strand | P26329 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 553 | 0.82 | 0.87 | 40 | empty |
| 2 | 119 | 0.48 | 0.80 | 16 | empty |
| 3 | 100 | 0.48 | 0.81 | 17 | empty |
| 4 | 94 | 0.41 | 0.77 | 23 | empty |
| 5 | 95 | 0.38 | 0.76 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 4215 Ų buried · 78 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2VSG · A Structural Motif in the Variant Surface Glycoproteins of Trypanosoma Brucei · the same entry in another collection · chain A against A, TM-score 1.00
- P26329 · AlphaFold monomer V2.0 prediction for variant surface glycoprotein iltat 1.24 (P26329) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P26329
- Elsewhere: RCSB PDB 2VSG · PDBe 2VSG · UniProt P26329
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