Research workbench
DNA replication protein
Analyse DNA replication protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GHT
- Type
- protein
- Length
- 467 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.795
- Source
- Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
- Molecule
- SsDNA-specific exonuclease
- UniProt
- Q5JGL0
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · resolution 2.795 · 1 distinct chain · 50% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SsDNA-specific exonuclease | protein | 467 | 50% helix, 16% strand | Q5JGL0 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 111 | 0.40 | 0.76 | 16 | empty |
| 2 | 97 | 0.36 | 0.74 | 18 | empty |
Compared structures
- 5GHT · DNA replication protein · 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 Q5JGL0
- Elsewhere: RCSB PDB 5GHT · PDBe 5GHT · UniProt Q5JGL0
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