Research workbench
Crystal structure of C-terminal domain of the human DNA primase large subunit with bound DNA TEMPLATE/RNA primer
Analyse Crystal structure of C-terminal domain of the human DNA primase large subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5F0Q
- Type
- protein + DNA + RNA
- Length
- 406 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA primase large subunit; RNA (5'-R(P*GP*GP*CP*GP*GP*C)-3'); DNA…
- EC
- 2.7.7.-
- UniProt
- P49643
- Ligands
- SF4, MG
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 5 distinct chains · 64% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA primase large subunit (EC 2.7.7.-) | protein | 187 | 65% helix, 1% strand | P49643 |
| B | DNA primase large subunit (EC 2.7.7.-) | protein | 185 | 64% helix, 0% strand | P49643 |
| C, E | RNA (5'-R(P*GP*GP*CP*GP*GP*C)-3') | rna | 6 | — | — |
| D | DNA (5'-D(*GP*CP*CP*GP*CP*CP*AP*AP*CP*AP*TP*A)-3') | dna | 12 | — | — |
| F | DNA (5'-D(*GP*CP*CP*GP*CP*CP*AP*AP*CP*AP*TP*A)-3') | dna | 10 | — | — |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, C, B, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.72 | 0.99 | 18 | SF4 |
| 2 | 587 | 0.72 | 0.80 | 49 | empty |
| 3 | 300 | 0.67 | 0.82 | 29 | MG |
| 4 | 279 | 0.67 | 0.83 | 27 | MG |
| 5 | 86 | 0.48 | 0.82 | 13 | empty |
Interfaces
7 interfaces between chains.
- A–D · 934 Ų buried · 20 hydrogen bonds · protein-nucleic
- B–F · 727 Ų buried · 14 hydrogen bonds · protein-nucleic
- A–B · 468 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 311 Ų buried · 32 hydrogen bonds · nucleic-nucleic
- E–F · 308 Ų buried · 27 hydrogen bonds · nucleic-nucleic
Modifications
Observed in the structure: 2 modified (nucleotide modification).
Compared structures
- 5F0Q · Crystal structure of C-terminal domain of the human DNA primase large subunit with bound… · the same entry in another collection · chain F against F, TM-score 1.00
- P49643 · AlphaFold monomer V2.0 prediction for DNA primase large subunit (P49643) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P49643
- Elsewhere: RCSB PDB 5F0Q · PDBe 5F0Q · UniProt P49643
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.