MolNFT v1 · #191784 · protein
AlphaFold monomer V2.0 prediction for RAS GTPase-activating-like protein IQGAP1 (P46940)
P46940: “AlphaFold monomer V2.0 prediction for RAS GTPase-activating-like protein IQGAP1 (P46940)”. MolNFT v1 #191784 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P46940
- Type
- protein
- Length
- 1,657 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- UniProt
- P46940
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1657 | — | P46940 |
Compared structures
- 3FAY · Crystal structure of the gap-related domain of IQGAP1 · an experimental structure of the same protein · chain A against A, TM-score 0.22
- 3FAY · Crystal structure of the GAP-related domain of IQGAP1 · an experimental structure of the same protein · chain A against A, TM-score 0.22
- 3I6X · Crystal structure of the calponin homology domain of IQGAP1 · an experimental structure of the same protein · chain A against A, TM-score 0.10
- 3I6X · Crystal structure of the calponin homology domain of IQGAP1 · an experimental structure of the same protein · chain A against A, TM-score 0.10
- 5L0O · IQGAP1 calponin homology domain fragment (CHDF) mutant K161C under oxidizing conditions · an experimental structure of the same protein · chain A against A, TM-score 0.10
- 5L0O · IQGAP1 calponin homology domain fragment (chdf) mutant K161C under oxidizing conditions · an experimental structure of the same protein · chain A against A, TM-score 0.10
- 1X0H · Solution structure of the carboxyl-terminal RGC domain in human IQGAP1 · an experimental structure of the same protein · chain A against A, TM-score 0.06
- 1X0H · Solution structure of the carboxyl-terminal rgc domain in human IQGAP1 · an experimental structure of the same protein · chain A against A, TM-score 0.06
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 P46940
- Elsewhere: UniProt P46940 · AlphaFold DB P46940
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