Research workbench
Crystal structure of the cancer genomic DNA mutator APOBEC3B with loop 7 from APOBEC3G complexed with 2-hp
Analyse Crystal structure of the cancer genomic DNA mutator APOBEC3B with loop 7 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NFL
- Type
- protein
- Length
- 182 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA dc->du-editing enzyme apobec-3B
- EC
- 3.5.4.38
- UniProt
- Q9UH17
- Ligands
- L60, 71O, CL
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA dc->du-editing enzyme apobec-3B (EC 3.5.4.38) | protein | 182 | 38% helix, 25% strand | Q9UH17 |
Ligands and binding sites
- L60 · 1,3-diazinan-2-one · ligand · chains A
- 71O · pyrimidin-2-ol · ligand · chains A
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6NFL · Crystal Structure of the Cancer Genomic DNA Mutator APOBEC3B with loop 7 from APOBEC3G… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UH17 · AlphaFold monomer V2.0 prediction for DNA dc->du-editing enzyme apobec-3B (Q9UH17) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q9UH17
- Elsewhere: RCSB PDB 6NFL · PDBe 6NFL · UniProt Q9UH17
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.