Research workbench
A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
Analyse A nucleotide-flipping mechanism from the structure of human uracil-DNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4SKN
- Type
- protein + DNA
- Length
- 242 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P13051
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | dna | 9 | — | — |
| B | — | dna | 10 | — | — |
| E | — | protein | 223 | — | P13051 |
Compared structures
- 4SKN · A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound… · the same entry in another collection · chain A against A, TM-score 1.00
- P13051 · AlphaFold monomer V2.0 prediction for uracil-DNA glycosylase (P13051) · a predicted model of the same protein · chain E against A, TM-score 0.98
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 P13051
- Elsewhere: RCSB PDB 4SKN · PDBe 4SKN · UniProt P13051
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