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Crystal structure of pasteurella multocida sialyltransferase D141N mutant in open conformation with cmp bound

Analyse Crystal structure of pasteurella multocida sialyltransferase D141N mutant in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2II6
Type: protein
Length: 393 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-2,3/2,6-SIALYLTRANSFERASE/SIALIDASE
EC: 2.4.99.4
UniProt: Q15KI8
Ligands: C5P
Pockets: 4 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-2,3/2,6-SIALYLTRANSFERASE/SIALIDASE (EC 2.4.99.4)	protein	393	41% helix, 18% strand	Q15KI8

Ligands and binding sites

C5P · Cytidine-5'-monophosphate · ligand · chains A

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

Pockets

4 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	355	0.59	0.76	47	C5P
2	79	0.42	0.79	16	empty
3	71	0.38	0.78	13	empty
4	67	0.36	0.78	21	empty

Compared structures

2II6 · Crystal structure of Pasteurella multocida sialyltransferase D141N mutant in open… · 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 2II6 · PDBe 2II6 · UniProt Q15KI8

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