MolNFT v1 · #167126 · protein
Human xpg endonuclease catalytic domain
6VBH · DNA repair protein complementing xp-G CELLS,FLAP…: “Human xpg endonuclease catalytic domain”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.69). MolNFT v1 #167126 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6VBH
- Type
- protein
- Length
- 326 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair protein complementing xp-G CELLS,FLAP endonuclease 1
- EC
- 3.1.-.-
- UniProt
- P28715, O93634
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair protein complementing xp-G CELLS,FLAP endonuclease 1 (EC 3.1.-.-) | protein | 326 | 50% helix, 9% strand | P28715, O93634 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 15 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 580 | 0.69 | 0.78 | 59 | SO4 |
| 2 | 119 | 0.48 | 0.79 | 20 | SO4 |
| 3 | 52 | 0.31 | 0.76 | 16 | SO4 |
Compared structures
- 6VBH · Human XPG endonuclease catalytic domain · the same entry in another collection · chain A against A, TM-score 1.00
- P28715 · AlphaFold monomer V2.0 prediction for DNA repair protein complementing xp-G cells (P28715) · a predicted model of the same protein · chain A against A, TM-score 0.88
- O93634 · AlphaFold monomer V2.0 prediction for flap endonuclease 1 (O93634) · a predicted model of the same protein · chain A against A, TM-score 0.73
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
- Every structure of UniProt O93634
- Elsewhere: RCSB PDB 6VBH · PDBe 6VBH · UniProt P28715 · UniProt O93634
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