Research workbench
Soluble adenylyl cyclase cyac from S. platensis in complex with rp-atpalphas in presence of bicarbonate
Analyse Soluble adenylyl cyclase cyac from S. platensis in complex with rp-atpalphas in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WC6
- Type
- protein
- Length
- 578 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenylate cyclase
- EC
- 4.6.1.1
- UniProt
- O32393
- Ligands
- TAT, MG
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Adenylate cyclase (EC 4.6.1.1) | protein | 193 | 34% helix, 35% strand | O32393 |
| B | Adenylate cyclase (EC 4.6.1.1) | protein | 192 | 34% helix, 35% strand | O32393 |
Ligands and binding sites
- TAT · Adenosine-5'-rp-alpha-thio-triphosphate · ligand · 3 copies · chains A, C, B
- MG · Magnesium ion · metal · 6 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 621 | 0.80 | 0.85 | 59 | TAT, MG |
| 2 | 486 | 0.77 | 0.85 | 55 | empty |
| 3 | 273 | 0.60 | 0.79 | 42 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1461 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 662 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 78 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1WC6 · Soluble adenylyl cyclase CyaC from S. platensis in complex with Rp- ATPalphaS in presence… · the same entry in another collection · chain A against A, TM-score 1.00
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 O32393
- Elsewhere: RCSB PDB 1WC6 · PDBe 1WC6 · UniProt O32393
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