Research workbench
Solution structure of the C1 domain of NORE1, a novel RAS effector
Analyse Solution structure of the C1 domain of NORE1, a novel RAS effector in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RFH
- Type
- protein
- Length
- 59 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS association (RALGDS/AF-6) domain family 5
- UniProt
- O70407
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 7% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS association (RALGDS/AF-6) domain family 5 | protein | 59 | 7% helix, 17% strand | O70407 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1RFH · Solution structure of the C1 domain of Nore1, a novel Ras effector · 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
- Every structure of UniProt O70407
- Elsewhere: RCSB PDB 1RFH · PDBe 1RFH · UniProt O70407
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