MolNFT v1 · #126409 · protein
Structure of a bacterial light-regulated adenylyl cylcase
5M27 · Beta subunit of photoactivated adenylyl cyclase: “Structure of a bacterial light-regulated adenylyl cylcase”. X-ray diffraction, 3 ligands (FMN, CA, CL), 10 pockets (best druggability 0.76). MolNFT v1 #126409 on GenesisL1: 3D…
- PDB
- 5M27
- Type
- protein
- Length
- 678 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta subunit of photoactivated adenylyl cyclase
- UniProt
- A7BT71
- Ligands
- FMN, CA, CL
- Pockets
- 10 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta subunit of photoactivated adenylyl cyclase | protein | 337 | 45% helix, 30% strand | A7BT71 |
| B | Beta subunit of photoactivated adenylyl cyclase | protein | 341 | 42% helix, 32% strand | A7BT71 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 914 | 0.76 | 0.79 | 82 | CA |
| 2 | 120 | 0.63 | 0.87 | 20 | FMN |
| 3 | 154 | 0.61 | 0.84 | 24 | FMN |
| 4 | 219 | 0.51 | 0.76 | 23 | empty |
| 5 | 66 | 0.47 | 0.83 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 3459 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 5M27 · Structure of a bacterial light-regulated adenylyl cylcase · 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 A7BT71
- Elsewhere: RCSB PDB 5M27 · PDBe 5M27 · UniProt A7BT71
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