Research workbench
Crystal structures of KDO8P synthase in its binary complexes with the mechanism-based inhibitor
Analyse Crystal structures of KDO8P synthase in its binary complexes with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G7V
- Type
- protein
- Length
- 284 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A715
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 284 | — | P0A715 |
Compared structures
- 1G7V · Crystal structures of KDO8P synthase in its binary complexes with the mechanism-based… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A715 · AlphaFold monomer V2.0 prediction for 2-dehydro-3-deoxyphosphooctonate aldolase (P0A715) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P0A715
- Elsewhere: RCSB PDB 1G7V · PDBe 1G7V · UniProt P0A715
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