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Cystal structure of dnag primase C-terminal domain from vibrio cholerae
Analyse Cystal structure of dnag primase C-terminal domain from vibrio cholerae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IM9
- Type
- protein
- Length
- 401 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- C3LX44
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 132 | — | C3LX44 |
| B | — | protein | 135 | — | C3LX44 |
| C | — | protein | 134 | — | C3LX44 |
Compared structures
- 4IM9 · Cystal structure of DnaG primase C-terminal domain from Vibrio cholerae · the same entry in another collection · chain A against A, TM-score 1.00
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 C3LX44
- Elsewhere: RCSB PDB 4IM9 · PDBe 4IM9 · UniProt C3LX44
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