Research workbench
Solution structure of CDC42HS complexed with a peptide derived from P- 21 activated kinase, NMR, 20 structures
Analyse Solution structure of CDC42HS complexed with a peptide derived from P- 21… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EES
- Type
- protein
- Length
- 224 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP-binding protein; P21-activated kinase
- UniProt
- P60953, Q61036
- Pockets
- 4 · best druggability 0.63
Structure
solution nmr · 2 distinct chains · 21% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP-binding protein | protein | 178 | 24% helix, 13% strand | P60953 |
| B | P21-activated kinase | protein | 46 | 9% helix, 0% strand | Q61036 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 249 | 0.63 | 0.81 | 38 | empty |
| 2 | 195 | 0.60 | 0.81 | 34 | empty |
| 3 | 50 | 0.42 | 0.83 | 20 | empty |
| 4 | 79 | 0.41 | 0.79 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2010 Ų buried · 41 hydrogen bonds · protein-protein
Compared structures
- 1EES · Solution structure of CDC42HS complexed with a peptide derived from P-21 activated… · the same entry in another collection · chain A against A, TM-score 1.00
- P60953 · AlphaFold monomer V2.0 prediction for cell division control protein 42 homolog (P60953) · a predicted model of the same protein · chain A against A, TM-score 0.63
- Q61036 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase pak 3 (Q61036) · a predicted model of the same protein · chain B against A, TM-score 0.33
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 P60953
- Every structure of UniProt Q61036
- Elsewhere: RCSB PDB 1EES · PDBe 1EES · UniProt P60953 · UniProt Q61036
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