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Crystal structure of pasteurella multocida sialyltransferase D141N mutant with cmp bound

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

PDB: 2IIB
Type: protein
Length: 377 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 0.65

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 2.4.99.4)	protein	377	42% helix, 19% 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	394	0.65	0.79	42	C5P
2	76	0.50	0.84	17	empty
3	58	0.34	0.78	13	empty
4	54	0.29	0.75	17	empty

Compared structures

2IIB · Crystal structure of Pasteurella multocida sialyltransferase D141N 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 2IIB · PDBe 2IIB · UniProt Q15KI8

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