Research workbench
Solution structure of the cysteine-rich C1 domain of kinase suppressor of RAS
Analyse Solution structure of the cysteine-rich C1 domain of kinase suppressor of RAS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KBF
- Type
- protein
- Length
- 49 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinase suppressor of RAS 1
- EC
- 2.7.11.1
- UniProt
- Q61097
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 0% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinase suppressor of RAS 1 (EC 2.7.11.1) | protein | 49 | 0% helix, 22% strand | Q61097 |
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.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1KBF · Solution Structure of the Cysteine-Rich C1 Domain of Kinase Suppressor of Ras · the same entry in another collection · chain A against A, TM-score 1.00
- Q61097 · AlphaFold monomer V2.0 prediction for kinase suppressor of RAS 1 (Q61097) · a predicted model of the same protein · chain A against A, TM-score 0.58
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 Q61097
- Elsewhere: RCSB PDB 1KBF · PDBe 1KBF · UniProt Q61097
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