Research workbench
Helical folded domain of mouse CAP1
Analyse Helical folded domain of mouse CAP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RSQ
- Type
- protein
- Length
- 703 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenylyl cyclase-associated protein 1
- UniProt
- P40124
- Pockets
- 6 · best druggability 0.54
Structure
x-ray diffraction · 4 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenylyl cyclase-associated protein 1 | protein | 173 | 77% helix, 1% strand | P40124 |
| B | Adenylyl cyclase-associated protein 1 | protein | 176 | 77% helix, 0% strand | P40124 |
| C | Adenylyl cyclase-associated protein 1 | protein | 175 | 77% helix, 0% strand | P40124 |
| D | Adenylyl cyclase-associated protein 1 | protein | 179 | 75% helix, 0% strand | P40124 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains A, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 214 | 0.54 | 0.78 | 28 | empty |
| 2 | 172 | 0.46 | 0.75 | 22 | empty |
| 3 | 114 | 0.45 | 0.78 | 16 | empty |
| 4 | 95 | 0.42 | 0.78 | 14 | GOL |
| 5 | 81 | 0.40 | 0.78 | 16 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1708 Ų buried · 24 hydrogen bonds · protein-protein
- A–D · 1556 Ų buried · 24 hydrogen bonds · protein-protein
- C–D · 258 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 P40124
- Elsewhere: RCSB PDB 6RSQ · PDBe 6RSQ · UniProt P40124
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