Research workbench
High resolution crystal structure of histidine triad nucleotide- binding protein 1 (HINT1) double cysteine mutant from rabbit
Analyse High resolution crystal structure of histidine triad nucleotide- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3O1Z
- Type
- protein
- Length
- 115 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine triad nucleotide-binding protein 1
- EC
- 3.-.-.-
- UniProt
- P80912
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine triad nucleotide-binding protein 1 (EC 3.-.-.-) | protein | 115 | 29% helix, 23% strand | P80912 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.30 | 0.73 | 18 | empty |
Compared structures
- 3O1Z · High resolution crystal structure of histidine triad nucleotide-binding protein 1 (Hint1)… · the same entry in another collection · chain A against A, TM-score 1.00
- P80912 · AlphaFold monomer V2.0 prediction for histidine triad nucleotide- binding protein 1… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P80912
- Elsewhere: RCSB PDB 3O1Z · PDBe 3O1Z · UniProt P80912
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