MolNFT v2 · #216462 · protein
Crystal structure of human Histidine Triad Nucleotide-Binding Protein 1 in complex with 5'-O-[N-(3-Indolepropionic acid)sulfamoyl] N2-methyl-2-aminoethenoadenosine
8PAI: “Crystal structure of human Histidine Triad Nucleotide-Binding Protein 1 in complex with…”. X-ray diffraction at 1.8, 1 ligand (XKO), 2 pockets (best druggability 0.36). MolNFT v2 #216462 on GenesisL1: 3D structure, binding sites and…
- PDB
- 8PAI
- Type
- protein
- Length
- 228 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Homo sapiens
- Molecule
- Histidine triad nucleotide-binding protein 1
- EC
- 3.-.-.-
- UniProt
- P49773
- Ligands
- XKO
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · resolution 1.8 · 2 distinct chains · 29% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine triad nucleotide-binding protein 1 (EC 3.-.-.-) | protein | 116 | 28% helix, 24% strand | P49773 |
| B | Histidine triad nucleotide-binding protein 1 (EC 3.-.-.-) | protein | 112 | 29% helix, 25% strand | P49773 |
Ligands and binding sites
- XKO · 5'-O-[N-(3-Indolepropionic acid)sulfamoyl] N2-methyl-2-aminoethenoadenosine · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.36 | 0.75 | 21 | empty |
| 2 | 82 | 0.36 | 0.75 | 22 | XKO |
Interfaces
1 interface between chains.
- A–B · 2010 Ų buried · 49 hydrogen bonds · protein-protein
Compared structures
- P49773 · AlphaFold monomer V2.0 prediction for histidine triad nucleotide- binding protein 1… · a predicted model of the same protein · chain B 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 P49773
- Elsewhere: RCSB PDB 8PAI · PDBe 8PAI · UniProt P49773
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