Research workbench
Structural analysis of the C-terminal domain of murine cmp-sialic acid synthetase
Analyse Structural analysis of the C-terminal domain of murine cmp-sialic acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EWI
- Type
- protein
- Length
- 315 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q99KK2
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 157 | — | Q99KK2 |
| B | — | protein | 158 | — | Q99KK2 |
Compared structures
- 3EWI · Structural analysis of the C-terminal domain of murine CMP-Sialic acid Synthetase · the same entry in another collection · chain A against A, TM-score 1.00
- Q99KK2 · AlphaFold monomer V2.0 prediction for N-acylneuraminate cytidylyltransferase (Q99KK2) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q99KK2
- Elsewhere: RCSB PDB 3EWI · PDBe 3EWI · UniProt Q99KK2
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