Research workbench
Open and closed structures of the udp-glucose pyrophosphorylase from leishmania major
Analyse Open and closed structures of the udp-glucose pyrophosphorylase from leishmania… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OEG
- Type
- protein
- Length
- 482 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q4QDU3
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 482 | — | Q4QDU3 |
Compared structures
- 2OEG · Open and Closed Structures of the UDP-Glucose Pyrophosphorylase from Leishmania major · 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 Q4QDU3
- Elsewhere: RCSB PDB 2OEG · PDBe 2OEG · UniProt Q4QDU3
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