Research workbench
Crystal structure of the PRI1 subunit of human primase bound to vidarabine triphosphate
Analyse Crystal structure of the PRI1 subunit of human primase bound to vidarabine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R4T
- Type
- protein
- Length
- 769 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P49642
- Ligands
- HEJ, ZN, MN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 384 | — | P49642 |
| D | — | protein | 385 | — | P49642 |
Ligands and binding sites
- HEJ · 9-{5-O-[(S)-hydroxy{[(r)-hydroxy(phosphonooxy) phosphoryl]oxy}phosphoryl]-beta-D-arabinofuranosyl}-9H-purin-6-amine · ligand · 2 copies · chains A, D
- ZN · Zinc ion · metal · 2 copies · chains A, D
- MN · Manganese (II) ion · metal · 2 copies · chains A, D
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6R4T · Crystal structure of the Pri1 subunit of human primase bound to vidarabine triphosphate · the same entry in another collection · chain A against A, TM-score 1.00
- P49642 · AlphaFold monomer V2.0 prediction for DNA primase small subunit (P49642) · a predicted model of the same protein · chain D against A, TM-score 0.97
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 P49642
- Elsewhere: RCSB PDB 6R4T · PDBe 6R4T · UniProt P49642
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