Research workbench
RB69 single-stranded DNA binding protein-DNA polymerase fusion
Analyse RB69 single-stranded DNA binding protein-DNA polymerase fusion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ATQ
- Type
- protein
- Length
- 1,055 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA polymerase; GP32
- EC
- 2.7.7.7
- UniProt
- Q38087, Q7Y265
- Ligands
- GDP, ZN
- Pockets
- 11 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA polymerase (EC 2.7.7.7) | protein | 845 | 38% helix, 14% strand | Q38087 |
| B | GP32 | protein | 210 | 20% helix, 21% strand | Q7Y265 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 658 | 0.72 | 0.79 | 65 | empty |
| 2 | 369 | 0.58 | 0.76 | 41 | empty |
| 3 | 163 | 0.57 | 0.82 | 33 | empty |
| 4 | 317 | 0.56 | 0.76 | 28 | empty |
| 5 | 117 | 0.54 | 0.82 | 18 | GDP |
Interfaces
1 interface between chains.
- A–B · 73 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2ATQ · RB69 single-stranded DNA binding protein-DNA polymerase fusion · 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 Q38087
- Every structure of UniProt Q7Y265
- Elsewhere: RCSB PDB 2ATQ · PDBe 2ATQ · UniProt Q38087 · UniProt Q7Y265
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