MolNFT v1 · #170983 · protein
Putative adenylyl cyclase HPAC1 from hippeastrum reveals a dominant triphophatase activity
6YP4 · Adenylate cyclase: “Putative adenylyl cyclase HPAC1 from hippeastrum reveals a dominant triphophatase activity”. X-ray diffraction, 3 ligands (GCP, MG, CL), 2 pockets (best druggability 0.69). MolNFT v1 #170983 on GenesisL1: 3D…
- PDB
- 6YP4
- Type
- protein
- Length
- 210 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenylate cyclase
- UniProt
- E1AQY1
- Ligands
- GCP, MG, CL
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenylate cyclase | protein | 210 | 32% helix, 42% strand | E1AQY1 |
Ligands and binding sites
- GCP · Phosphomethylphosphonic acid guanylate ester · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 318 | 0.69 | 0.83 | 47 | GCP, MG, CL |
| 2 | 77 | 0.51 | 0.84 | 23 | EDO |
Compared structures
- 6YP4 · Putative adenylyl cyclase HpAC1 from Hippeastrum reveals a dominant triphophatase activity · 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 E1AQY1
- Elsewhere: RCSB PDB 6YP4 · PDBe 6YP4 · UniProt E1AQY1
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