Research workbench
Solution structure of the pH domain of PIP2-dependent ARF1 GTPase- activating protein from human
Analyse Solution structure of the pH domain of PIP2-dependent ARF1 GTPase- activating… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DA0
- Type
- protein
- Length
- 114 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9ULH1
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 114 | — | Q9ULH1 |
Compared structures
- 2DA0 · Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ULH1 · AlphaFold monomer V2.0 prediction for arf-gap with SH3 domain, ank repeat and pH… · 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 Q9ULH1
- Elsewhere: RCSB PDB 2DA0 · PDBe 2DA0 · UniProt Q9ULH1
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