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Crystal structure of pasteurella multocida sialyltransferase M144D mutant with cmp bound

Analyse Crystal structure of pasteurella multocida sialyltransferase M144D mutant with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3S44
Type: protein
Length: 388 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-2,3/2,6-SIALYLTRANSFERASE/SIALIDASE
EC: 2.4.99.-
UniProt: Q15KI8
Ligands: FN5
Pockets: 3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-2,3/2,6-SIALYLTRANSFERASE/SIALIDASE (EC 2.4.99.-)	protein	388	42% helix, 19% strand	Q15KI8

Ligands and binding sites

FN5 · CMP-3F(a)-Neu5Ac · ligand · chains A

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

Pockets

3 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	298	0.55	0.76	48	FN5
2	94	0.41	0.77	16	empty
3	85	0.38	0.77	20	empty

Compared structures

3S44 · Crystal Structure of Pasteurella multocida sialyltransferase M144D mutant with CMP bound · the same entry in another collection · chain A against A, TM-score 1.00

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 Q15KI8
Elsewhere: RCSB PDB 3S44 · PDBe 3S44 · UniProt Q15KI8

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