Research workbench
Crystal structure of IIGP1: a paradigm for interferon inducible P47 resistance gtpases
Analyse Crystal structure of IIGP1: a paradigm for interferon inducible P47 resistance… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TQD
- Type
- protein
- Length
- 764 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interferon-inducible GTPase
- UniProt
- Q9QZ85
- Ligands
- SO4
- Pockets
- 13 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 56% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interferon-inducible GTPase | protein | 385 | 55% helix, 8% strand | Q9QZ85 |
| B | Interferon-inducible GTPase | protein | 379 | 56% helix, 9% strand | Q9QZ85 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 562 | 0.69 | 0.79 | 48 | empty |
| 2 | 477 | 0.67 | 0.79 | 42 | empty |
| 3 | 90 | 0.43 | 0.79 | 17 | empty |
| 4 | 99 | 0.41 | 0.77 | 24 | empty |
| 5 | 94 | 0.40 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1112 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1TQD · Crystal structure of IIGP1: a paradigm for interferon inducible p47 resistance GTPases · the same entry in another collection · chain A against A, TM-score 1.00
- Q9QZ85 · AlphaFold monomer V2.0 prediction for interferon-inducible GTPase 1 (Q9QZ85) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 Q9QZ85
- Elsewhere: RCSB PDB 1TQD · PDBe 1TQD · UniProt Q9QZ85
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