MolNFT v1 · #162300 · protein
Crystal structure of the PRI1 subunit of human primase bound to ATP
6R4S: “Crystal structure of the PRI1 subunit of human primase bound to ATP”. X-ray diffraction, 3 ligands (ATP, MN, ZN). MolNFT v1 #162300 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6R4S
- Type
- protein
- Length
- 765 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P49642
- Ligands
- ATP, MN, ZN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 382 | — | P49642 |
| E | — | protein | 383 | — | P49642 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, E
- MN · Manganese (II) ion · metal · 4 copies · chains A, E
- ZN · Zinc ion · metal · 2 copies · chains A, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6R4S · Crystal structure of the Pri1 subunit of human primase bound to ATP · 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 A 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 6R4S · PDBe 6R4S · UniProt P49642
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