Research workbench
Crystal structure of histidine triad nucleotide-binding protein 1 (HINT1) from human complexed with TRP-ams
Analyse Crystal structure of histidine triad nucleotide-binding protein 1 (HINT1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EQH
- Type
- protein
- Length
- 229 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine triad nucleotide-binding protein 1
- EC
- 3.-.-.-
- UniProt
- P49773
- Ligands
- WSA
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine triad nucleotide-binding protein 1 (EC 3.-.-.-) | protein | 114 | 29% helix, 25% strand | P49773 |
| B | Histidine triad nucleotide-binding protein 1 (EC 3.-.-.-) | protein | 115 | 29% helix, 24% strand | P49773 |
Ligands and binding sites
- WSA · 5'-O-[(L-tryptophylamino)sulfonyl]adenosine · ligand · chains A, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains 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 | 87 | 0.36 | 0.75 | 27 | WSA |
| 2 | 62 | 0.30 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1990 Ų buried · 43 hydrogen bonds · protein-protein
Compared structures
- 4EQH · Crystal structure of histidine triad nucleotide-binding protein 1 (HINT1) from human… · 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 4EQH · PDBe 4EQH · UniProt P49773
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