Research workbench
Solution structure of the helicase-binding domain of escherichia COLI primase
Analyse Solution structure of the helicase-binding domain of escherichia COLI primase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HAJ
- Type
- protein
- Length
- 135 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA primase
- EC
- 2.7.7.-
- UniProt
- P0ABS5
Structure
solution nmr · 1 distinct chain · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA primase (EC 2.7.7.-) | protein | 135 | 67% helix, 0% strand | P0ABS5 |
Compared structures
- 2HAJ · Solution structure of the helicase-binding domain of Escherichia coli primase · the same entry in another collection · chain A against A, TM-score 1.00
- P0ABS5 · AlphaFold monomer V2.0 prediction for DNA primase (P0ABS5) · 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 P0ABS5
- Elsewhere: RCSB PDB 2HAJ · PDBe 2HAJ · UniProt P0ABS5
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