Research workbench
IQGAP1 calponin homology domain fragment (chdf) mutant K161C under oxidizing conditions
Analyse IQGAP1 calponin homology domain fragment (chdf) mutant K161C under oxidizing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5L0O
- Type
- protein
- Length
- 656 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS GTPase-activating-like protein IQGAP1
- UniProt
- P46940
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | RAS GTPase-activating-like protein IQGAP1 | protein | 164 | 64% helix, 0% strand | P46940 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1145 | 0.73 | 0.76 | 87 | empty |
| 2 | 737 | 0.70 | 0.76 | 68 | empty |
| 3 | 92 | 0.50 | 0.82 | 24 | empty |
| 4 | 94 | 0.43 | 0.78 | 23 | empty |
Interfaces
4 interfaces between chains.
- C–D · 790 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 749 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 116 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 103 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5L0O · IQGAP1 calponin homology domain fragment (CHDF) mutant K161C under oxidizing conditions · the same entry in another collection · chain A against A, TM-score 1.00
- P46940 · AlphaFold monomer V2.0 prediction for RAS GTPase-activating-like protein IQGAP1 (P46940) · a predicted model of the same protein · chain A against A, TM-score 0.99
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: RCSB PDB 5L0O · PDBe 5L0O · UniProt P46940
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