Research workbench
Crystal structure of human soluble adenylyl cyclase with ALPHA,BETA- methyleneadenosine-5'-triphosphate soaked with bicarbonate
Analyse Crystal structure of human soluble adenylyl cyclase with ALPHA,BETA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CM0
- Type
- protein
- Length
- 461 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Soluble adenylyl cyclase
- EC
- 4.6.1.1
- UniProt
- Q96PN6
- Ligands
- APC, CA, CL
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Soluble adenylyl cyclase (EC 4.6.1.1) | protein | 461 | 39% helix, 28% strand | Q96PN6 |
Ligands and binding sites
- APC · Diphosphomethylphosphonic acid adenosyl ester · ligand · chains A
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 415 | 0.79 | 0.88 | 49 | APC, CA, CL |
| 2 | 231 | 0.76 | 0.90 | 31 | empty |
| 3 | 137 | 0.64 | 0.87 | 23 | empty |
| 4 | 171 | 0.47 | 0.76 | 22 | empty |
Modifications
Observed in the structure: 1 modified (artifact).
Compared structures
- 4CM0 · Crystal structure of human soluble Adenylyl Cyclase with alpha,beta… · 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 4CM0 · PDBe 4CM0 · UniProt Q96PN6
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