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Crystal structure of ALPHA1,3-fucosyltransferase

Analyse Crystal structure of ALPHA1,3-fucosyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NZW
Type: protein
Length: 1,038 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALPHA1,3-fucosyltransferase
EC: 2.4.1.152
UniProt: O30511
Ligands: SO4
Pockets: 16 · best druggability 0.80

Structure

x-ray diffraction · 3 distinct chains · 37% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ALPHA1,3-fucosyltransferase (EC 2.4.1.152)	protein	349	38% helix, 16% strand	O30511
B	ALPHA1,3-fucosyltransferase (EC 2.4.1.152)	protein	338	36% helix, 16% strand	O30511
C	ALPHA1,3-fucosyltransferase (EC 2.4.1.152)	protein	351	39% helix, 15% strand	O30511

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains B, C

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

Pockets

16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	820	0.80	0.83	86	empty
2	290	0.64	0.81	38	empty
3	277	0.60	0.79	29	empty
4	206	0.56	0.79	33	empty
5	207	0.56	0.79	32	empty

Interfaces

3 interfaces between chains.

A–C · 902 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 684 Å² buried · 9 hydrogen bonds · protein-protein
B–C · 378 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2NZW · Crystal Structure of alpha1,3-Fucosyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
O30511 · AlphaFold monomer V2.0 prediction for alpha-(1,3)-fucosyltransferase fuct (O30511) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 O30511
Elsewhere: RCSB PDB 2NZW · PDBe 2NZW · UniProt O30511

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