Research workbench
Pold-PCNA-DNA (form a)
Analyse Pold-PCNA-DNA (form a) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KNB
- Type
- protein + DNA
- Length
- 2,367 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA polymerase II small subunit; DNA polymerase D DP2 (DNA polymerase II large) subunit…
- EC
- 2.7.7.7, 3.1.11.1
- UniProt
- Q5JET1, Q5JF32
- Ligands
- ZN, FE
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 5 distinct chains · 33% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA polymerase II small subunit (EC 2.7.7.7, 3.1.11.1) | protein | 450 | 22% helix, 18% strand | Q5JET1 |
| B | DNA polymerase D DP2 (DNA polymerase II large) subunit | protein | 1120 | 41% helix, 11% strand | — |
| C, D, E | DNA polymerase sliding clamp 1 | protein | 249 | 17% helix, 45% strand | Q5JF32 |
| F | PRI25DNA | dna | 25 | — | — |
| G | TEMP35DNA | dna | 25 | — | — |
Ligands and binding sites
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 | 1049 | 0.86 | 0.87 | 126 | empty |
| 2 | 746 | 0.84 | 0.87 | 116 | empty |
| 3 | 400 | 0.83 | 0.91 | 70 | empty |
| 4 | 792 | 0.81 | 0.85 | 105 | empty |
| 5 | 497 | 0.81 | 0.88 | 78 | empty |
Interfaces
16 interfaces between chains.
- A–B · 1745 Ų buried · 12 hydrogen bonds · protein-protein
- F–G · 1165 Ų buried · 93 hydrogen bonds · nucleic-nucleic
- C–D · 729 Ų buried · 15 hydrogen bonds · protein-protein
- D–E · 704 Ų buried · 19 hydrogen bonds · protein-protein
- C–E · 647 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 Q5JET1
- Every structure of UniProt Q5JF32
- Elsewhere: RCSB PDB 6KNB · PDBe 6KNB · UniProt Q5JET1 · UniProt Q5JF32
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