Research workbench
Low resolution crystal structure of the NTF2-like domain of human G3BP1
Analyse Low resolution crystal structure of the NTF2-like domain of human G3BP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IIA
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS GTPase-activating protein-binding protein 1
- EC
- 3.6.4.12, 3.6.4.13
- UniProt
- Q13283
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS GTPase-activating protein-binding protein 1 (EC 3.6.4.12, 3.6.4.13) | protein | 131 | 28% helix, 37% strand | Q13283 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4IIA · Low resolution crystal structure of the NTF2-like domain of human G3BP1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q13283 · AlphaFold monomer V2.0 prediction for RAS GTPase-activating protein- binding protein 1… · 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 Q13283
- Elsewhere: RCSB PDB 4IIA · PDBe 4IIA · UniProt Q13283
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