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Structure of a sialic acid activating synthetase, cmp acylneuraminate synthetase in the presence and absence of cdp

Analyse Structure of a sialic acid activating synthetase, cmp acylneuraminate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1EZI
Type
protein
Length
429 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cmp-N-acetylneuraminic acid synthetase
EC
2.7.7.43
UniProt
P0A0Z8
Pockets
1 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACmp-N-acetylneuraminic acid synthetase (EC 2.7.7.43)protein21632% helix, 25% strandP0A0Z8
BCmp-N-acetylneuraminic acid synthetase (EC 2.7.7.43)protein21332% helix, 27% strandP0A0Z8

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18410.700.7588empty

Interfaces

1 interface between chains.

  • A–B · 1408 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

  • 1EZI · Structure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the… · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A0Z8 · AlphaFold monomer V2.0 prediction for N-acylneuraminate cytidylyltransferase (P0A0Z8) · a predicted model of the same protein · chain A against A, TM-score 0.96

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