MolNFT v1 · #129075 · protein
Crystal structure of human histamine-releasing factor (HRF/TCTP) containing a disulphide-linked dimer
5O9M · Translationally-controlled tumor protein: “Crystal structure of human histamine-releasing factor (HRF/TCTP) containing a disulphide-linked dimer”. X-ray diffraction, 2 pockets (best druggability 0.37). MolNFT v1 #129075 on…
- PDB
- 5O9M
- Type
- protein
- Length
- 321 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Translationally-controlled tumor protein
- UniProt
- P13693
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Translationally-controlled tumor protein | protein | 157 | 34% helix, 35% strand | P13693 |
| B | Translationally-controlled tumor protein | protein | 164 | 34% helix, 28% strand | P13693 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · 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 | 62 | 0.37 | 0.79 | 12 | empty |
| 2 | 60 | 0.35 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1017 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5O9M · Crystal structure of human Histamine-Releasing Factor (HRF/TCTP)containing a… · the same entry in another collection · chain A against A, TM-score 1.00
- P13693 · AlphaFold monomer V2.0 prediction for translationally-controlled tumor protein (P13693) · 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 P13693
- Elsewhere: RCSB PDB 5O9M · PDBe 5O9M · UniProt P13693
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