Research workbench
Crystal structure of MAP and CDC42 complex
Analyse Crystal structure of MAP and CDC42 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GCG
- Type
- protein
- Length
- 325 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division control protein 42 homolog; L0028 (mitochondria associated protein)
- UniProt
- P60953, Q9R8E4
- Pockets
- 5 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division control protein 42 homolog | protein | 173 | 34% helix, 23% strand | P60953 |
| B | L0028 (mitochondria associated protein) | protein | 152 | 73% helix, 0% strand | Q9R8E4 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.55 | 0.89 | 16 | empty |
| 2 | 224 | 0.53 | 0.77 | 28 | empty |
| 3 | 93 | 0.39 | 0.77 | 16 | empty |
| 4 | 92 | 0.37 | 0.75 | 18 | empty |
| 5 | 63 | 0.33 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1476 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
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 Q9R8E4
- Elsewhere: RCSB PDB 3GCG · PDBe 3GCG · UniProt P60953 · UniProt Q9R8E4
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