Research workbench
Human xpg-DNA, complex 1
Analyse Human xpg-DNA, complex 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TUW
- Type
- protein + DNA
- Length
- 331 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair protein complementing xp-G CELLS,DNA repair protein complementing xp-G cells…
- EC
- 3.1.-.-
- UniProt
- P28715
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 3 distinct chains · 51% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair protein complementing xp-G CELLS,DNA repair protein complementing xp-G cells (EC 3.1.-.-) | protein | 313 | 51% helix, 10% strand | P28715 |
| B | DNA (5'-D(P*TP*GP*CP*AP*GP*AP*GP*TP*TP*C)-3') | dna | 10 | — | — |
| C | DNA (5'-D(P*GP*AP*AP*CP*TP*CP*TP*G)-3') | dna | 8 | — | — |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 954 | 0.73 | 0.77 | 77 | empty |
| 2 | 143 | 0.48 | 0.78 | 22 | empty |
| 3 | 175 | 0.45 | 0.75 | 16 | empty |
Interfaces
3 interfaces between chains.
- B–C · 394 Ų buried · 35 hydrogen bonds · nucleic-nucleic
- A–B · 199 Ų buried · 1 hydrogen bond · protein-nucleic
- A–C · 165 Ų buried · 2 hydrogen bonds · protein-nucleic
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 P28715
- Elsewhere: RCSB PDB 6TUW · PDBe 6TUW · UniProt P28715
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