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Crystal structure of nicotinate-nucleotide pyrophosphorylase from ehrlichia chaffeensis at 2.05A resolution
Analyse Crystal structure of nicotinate-nucleotide pyrophosphorylase from ehrlichia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3L0G
- Type
- protein
- Length
- 1,093 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q2GI74
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 272 | — | Q2GI74 |
| B | — | protein | 273 | — | Q2GI74 |
| C | — | protein | 274 | — | Q2GI74 |
| D | — | protein | 274 | — | Q2GI74 |
Compared structures
- 3L0G · Crystal structure of Nicotinate-nucleotide pyrophosphorylase from Ehrlichia chaffeensis… · 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 Q2GI74
- Elsewhere: RCSB PDB 3L0G · PDBe 3L0G · UniProt Q2GI74
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