Research workbench
Re-investigated high resolution crystal structure of histidine triad nucleotide-binding protein 1 (HINT1) from rabbit complexed with adenosine
Analyse Re-investigated high resolution crystal structure of histidine triad… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QGZ
- Type
- protein
- Length
- 114 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
- Ligands
- ADN
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine triad nucleotide-binding protein 1 (EC 3.-.-.-) | protein | 114 | 29% helix, 22% strand | P80912 |
Ligands and binding sites
- ADN · Adenosine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3QGZ · Re-investigated high resolution crystal structure of histidine triad nucleotide-binding… · 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 0.97
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 3QGZ · PDBe 3QGZ · UniProt P80912
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.