MolNFT v1 · #180960 · protein
Synechocystis sp. UTEX2470 cyanophycin synthetase 1 with ATP
7LG5 · Cyanophycin synthase: “Synechocystis sp. UTEX2470 cyanophycin synthetase 1 with ATP”. Electron microscopy, 2 ligands (ATP, MG), 20 pockets (best druggability 0.75). MolNFT v1 #180960 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7LG5
- Type
- protein
- Length
- 3,484 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyanophycin synthase
- EC
- 6.3.2.29, 6.3.2.30
- UniProt
- A0A068N621
- Ligands
- ATP, MG
- Pockets
- 20 · best druggability 0.75
Structure
electron microscopy · 1 distinct chain · 32% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Cyanophycin synthase (EC 6.3.2.29, 6.3.2.30) | protein | 871 | 32% helix, 22% strand | A0A068N621 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 8 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 12 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 907 | 0.75 | 0.79 | 90 | ATP, MG |
| 2 | 935 | 0.74 | 0.78 | 79 | ATP, MG |
| 3 | 862 | 0.73 | 0.78 | 68 | ATP, MG |
| 4 | 885 | 0.73 | 0.77 | 73 | ATP, MG |
| 5 | 610 | 0.72 | 0.80 | 61 | ATP, MG |
Interfaces
4 interfaces between chains.
- A–B · 1839 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1829 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 486 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 480 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 7LG5 · Synechocystis sp. UTEX2470 Cyanophycin synthetase 1 with ATP · 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 A0A068N621
- Elsewhere: RCSB PDB 7LG5 · PDBe 7LG5 · UniProt A0A068N621
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