Research workbench
The solution structure of the brct domain from human polymerase reveals homology with the tdt brct domain
Analyse The solution structure of the brct domain from human polymerase reveals… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HTF
- Type
- protein
- Length
- 105 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA polymerase mu
- EC
- 2.7.7.7
- UniProt
- Q9NP87
Structure
solution nmr · 1 distinct chain · 38% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA polymerase mu (EC 2.7.7.7) | protein | 105 | 38% helix, 14% strand | Q9NP87 |
Compared structures
- 2HTF · The solution structure of the BRCT domain from human polymerase reveals homology with the… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NP87 · AlphaFold monomer V2.0 prediction for DNA-directed DNA/RNA polymerase mu (Q9NP87) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 Q9NP87
- Elsewhere: RCSB PDB 2HTF · PDBe 2HTF · UniProt Q9NP87
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