Research workbench
The crystal structure of apo domain-swapped dimer Q108K:T51D:I32C variant of hcrbpii with an engineered disulfide bond
Analyse The crystal structure of apo domain-swapped dimer Q108K:T51D:I32C variant of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VIT
- Type
- protein
- Length
- 266 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinol-binding protein 2
- UniProt
- P50120
- Pockets
- 2 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Retinol-binding protein 2 | protein | 133 | 10% helix, 57% strand | P50120 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 323 | 0.85 | 0.95 | 43 | empty |
| 2 | 247 | 0.84 | 0.96 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 4013 Ų buried · 73 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6VIT · The Crystal Structure of Apo Domain-Swapped dimer Q108K:T51D:I32C Variant of HCRBPII with… · 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 P50120
- Elsewhere: RCSB PDB 6VIT · PDBe 6VIT · UniProt P50120
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.