Research workbench
Structure of C-terminal coiled coil of RASGRP1
Analyse Structure of C-terminal coiled coil of RASGRP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L9U
- Type
- protein
- Length
- 91 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS guanyl-releasing protein 1
- UniProt
- O95267
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 85% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS guanyl-releasing protein 1 | protein | 49 | 80% helix, 0% strand | O95267 |
| B | RAS guanyl-releasing protein 1 | protein | 42 | 90% helix, 0% strand | O95267 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1111 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
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 O95267
- Elsewhere: RCSB PDB 4L9U · PDBe 4L9U · UniProt O95267
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