MolNFT v1 · #104659 · protein
Crystal structure of apo human APE1
4QHD · DNA-(apurinic or apyrimidinic site) lyase: “Crystal structure of apo human APE1”. X-ray diffraction, 4 pockets (best druggability 0.46). MolNFT v1 #104659 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4QHD
- Type
- protein
- Length
- 281 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-(apurinic or apyrimidinic site) lyase
- EC
- 3.1.-.-, 4.2.99.18
- UniProt
- P27695
- Pockets
- 4 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-, 4.2.99.18) | protein | 281 | 26% helix, 24% strand | P27695 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.46 | 0.75 | 32 | EDO |
| 2 | 58 | 0.34 | 0.77 | 16 | empty |
| 3 | 50 | 0.33 | 0.78 | 12 | empty |
| 4 | 74 | 0.33 | 0.75 | 21 | empty |
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 P27695
- Elsewhere: RCSB PDB 4QHD · PDBe 4QHD · UniProt P27695
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