Research workbench
Crystal structure of a tat-interacting protein homologue (HTATIP2, AW111545, CC3, TIP30) from mus musculus at 2.30 a resolution
Analyse Crystal structure of a tat-interacting protein homologue (HTATIP2, AW111545… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FMU
- Type
- protein
- Length
- 209 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIV-1 tat interactive protein 2, 30 kda homolog
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HIV-1 tat interactive protein 2, 30 kda homolog | protein | 209 | 45% helix, 20% strand | — |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.51 | 0.81 | 21 | empty |
| 2 | 68 | 0.38 | 0.79 | 18 | empty |
| 3 | 104 | 0.36 | 0.74 | 19 | empty |
Compared structures
- 2FMU · Crystal structure of a tat-interacting protein homologue (htatip2, aw111545, cc3, tip30)… · 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
- Elsewhere: RCSB PDB 2FMU · PDBe 2FMU
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