Research workbench
Crystal structure of human soluble adenylyl cyclase in complex with ALPHA,BETA-methyleneadenosine-5'-triphosphate
Analyse Crystal structure of human soluble adenylyl cyclase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4USU
- Type
- protein
- Length
- 464 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenylate cyclase type 10
- EC
- 4.6.1.1
- UniProt
- Q96PN6
- Ligands
- APC, CA, CL
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenylate cyclase type 10 (EC 4.6.1.1) | protein | 464 | 38% helix, 29% strand | Q96PN6 |
Ligands and binding sites
- APC · Diphosphomethylphosphonic acid adenosyl ester · ligand · chains A
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.76 | 0.89 | 32 | CL, EDO |
| 2 | 351 | 0.73 | 0.85 | 45 | APC, CA |
| 3 | 59 | 0.70 | 0.97 | 17 | CL |
| 4 | 143 | 0.66 | 0.88 | 24 | EDO |
| 5 | 195 | 0.48 | 0.76 | 27 | empty |
Modifications
Observed in the structure: 1 modified (artifact).
Compared structures
- 4USU · Crystal structure of human soluble Adenylyl Cyclase in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q96PN6 · AlphaFold monomer V2.0 prediction for adenylate cyclase type 10 (Q96PN6) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q96PN6
- Elsewhere: RCSB PDB 4USU · PDBe 4USU · UniProt Q96PN6
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