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Crystal structure analysis of monofunctional alpha-2,3- sialyltransferase cst-I from campylobacter jejuni

Analyse Crystal structure analysis of monofunctional alpha-2,3- sialyltransferase cst-I… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2P2V
Type: protein
Length: 275 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-2,3-sialyltransferase
EC: 2.4.99.-
UniProt: Q9RGF1
Ligands: CSF, CL
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-2,3-sialyltransferase (EC 2.4.99.-)	protein	275	39% helix, 13% strand	Q9RGF1

Ligands and binding sites

CSF · Cytidine-5'-monophosphate-3-fluoro-N-acetyl-neuraminic acid · ligand · chains A
CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · additive · 12 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	549	0.74	0.82	60	EDO, CSF
2	63	0.35	0.77	10	empty

Compared structures

2P2V · Crystal structure analysis of monofunctional alpha-2,3-sialyltransferase Cst-I from… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt Q9RGF1
Elsewhere: RCSB PDB 2P2V · PDBe 2P2V · UniProt Q9RGF1

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