MolNFT v1 · #186817 · protein
Structure of deep-sea phage nrs-1 primase-polymerase N300 in complex with calcium and ddctp
7RR3: “Structure of deep-sea phage nrs-1 primase-polymerase N300 in complex with calcium and ddctp”. X-ray diffraction, 2 ligands (DCT, CA), 1 pocket (best druggability 0.43). MolNFT v1 #186817 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7RR3
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Primase
- UniProt
- M5AAG8
- Ligands
- DCT, CA
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Primase | protein | 275 | 31% helix, 22% strand | M5AAG8 |
Ligands and binding sites
- DCT · 2',3'-dideoxycytidine 5'-triphosphate · ligand · chains A
- CA · Calcium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.43 | 0.77 | 19 | CA, DCT |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 7RR3 · Structure of Deep-Sea Phage NrS-1 Primase-Polymerase N300 in complex with calcium and… · 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 M5AAG8
- Elsewhere: RCSB PDB 7RR3 · PDBe 7RR3 · UniProt M5AAG8
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