Research workbench
NMR structures of the zinc finger domain of human DNA polymerase-alpha
Analyse NMR structures of the zinc finger domain of human DNA polymerase-alpha in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K0P
- Type
- protein
- Length
- 31 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA polymerase alpha catalytic subunit
- EC
- 2.7.7.7
- UniProt
- P09884
Structure
solution nmr · 1 distinct chain · 29% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA polymerase alpha catalytic subunit (EC 2.7.7.7) | protein | 31 | 29% helix, 0% strand | P09884 |
Compared structures
- 1K0P · NMR Structures of the Zinc Finger Domain of Human DNA Polymerase-alpha · the same entry in another collection · chain A against A, TM-score 1.00
- P09884 · AlphaFold monomer V2.0 prediction for DNA polymerase alpha catalytic subunit (P09884) · a predicted model of the same protein · chain A against A, TM-score 0.38
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 P09884
- Elsewhere: RCSB PDB 1K0P · PDBe 1K0P · UniProt P09884
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