Research workbench
2.55 ångström resolution structure of 3-phosphoshikimate 1- carboxyvinyltransferase (aroa) from coxiella burnetii in complex with shikimate-3-phosphate, phosphate, and potassium
Analyse 2.55 ångström resolution structure of 3-phosphoshikimate 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZND
- Type
- protein
- Length
- 436 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q83E11
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 436 | — | Q83E11 |
Compared structures
- 4ZND · 2.55 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA)… · the same entry in another collection · chain A against A, TM-score 1.00
- Q83E11 · AlphaFold monomer V2.0 prediction for 3-phosphoshikimate 1-carboxyvinyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q83E11
- Elsewhere: RCSB PDB 4ZND · PDBe 4ZND · UniProt Q83E11
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