Research workbench
Crystal structure of human histidine triad nucleotide-binding protein 1 (HHINT1) refined to 1.92A at P21 space group
Analyse Crystal structure of human histidine triad nucleotide-binding protein 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZKV
- Type
- protein
- Length
- 460 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine triad nucleotide-binding protein 1
- EC
- 3.-.-.-
- UniProt
- P49773
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Histidine triad nucleotide-binding protein 1 (EC 3.-.-.-) | protein | 115 | 29% helix, 25% strand | P49773 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 156 | 0.50 | 0.78 | 29 | empty |
| 2 | 198 | 0.48 | 0.75 | 38 | SO4 |
| 3 | 72 | 0.35 | 0.76 | 21 | empty |
| 4 | 70 | 0.34 | 0.75 | 20 | empty |
| 5 | 66 | 0.31 | 0.74 | 21 | SO4 |
Interfaces
3 interfaces between chains.
- A–B · 2030 Ų buried · 46 hydrogen bonds · protein-protein
- C–D · 2016 Ų buried · 48 hydrogen bonds · protein-protein
- B–C · 362 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 4ZKV · Crystal structure of human histidine triad nucleotide-binding protein 1 (hHINT1) refined… · 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 P49773
- Elsewhere: RCSB PDB 4ZKV · PDBe 4ZKV · UniProt P49773
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