Research workbench
Solution structure of the second SH2 domain of human RAS GTPase- activating protein 1
Analyse Solution structure of the second SH2 domain of human RAS GTPase- activating… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GSB
- Type
- protein
- Length
- 119 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS GTPase-activating protein 1
- UniProt
- P20936
Structure
solution nmr · 1 distinct chain · 18% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS GTPase-activating protein 1 | protein | 119 | 18% helix, 21% strand | P20936 |
Compared structures
- 2GSB · Solution structure of the second SH2 domain of human Ras GTPase-activating protein 1 · the same entry in another collection · chain A against A, TM-score 1.00
- P20936 · AlphaFold monomer V2.0 prediction for RAS GTPase-activating protein 1 (P20936) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 P20936
- Elsewhere: RCSB PDB 2GSB · PDBe 2GSB · UniProt P20936
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