MolNFT v1 · #115300 · protein
C2 crystal form of APE1 with MG2+
5CFG · DNA-(apurinic or apyrimidinic site) lyase: “C2 crystal form of APE1 with MG2+”. X-ray diffraction, 1 ligand (MG), 2 pockets (best druggability 0.46). MolNFT v1 #115300 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5CFG
- Type
- protein
- Length
- 275 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
- Ligands
- MG
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 31% 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 | 275 | 31% helix, 24% strand | P27695 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 170 | 0.46 | 0.76 | 35 | empty |
| 2 | 64 | 0.36 | 0.78 | 13 | 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 5CFG · PDBe 5CFG · UniProt P27695
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