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Alpha-L-fucosidase alfc fucosyltransferase mutant E274A

Analyse Alpha-L-fucosidase alfc fucosyltransferase mutant E274A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6O1I
Type: protein
Length: 1,296 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alfc
EC: 3.2.1.51
UniProt: K0NB39
Pockets: 16 · best druggability 0.75

Structure

x-ray diffraction · 4 distinct chains · 36% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alfc (EC 3.2.1.51)	protein	328	36% helix, 15% strand	K0NB39
B	Alfc (EC 3.2.1.51)	protein	322	37% helix, 15% strand	K0NB39
C	Alfc (EC 3.2.1.51)	protein	324	37% helix, 15% strand	K0NB39
D	Alfc (EC 3.2.1.51)	protein	322	36% helix, 15% strand	K0NB39

Pockets

16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	63	0.75	0.99	16	empty
2	57	0.72	0.98	16	empty
3	332	0.67	0.81	38	empty
4	407	0.67	0.80	54	empty
5	258	0.66	0.82	33	empty

Interfaces

3 interfaces between chains.

A–C · 1244 Å² buried · 12 hydrogen bonds · protein-protein
B–D · 1243 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 344 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6O1I · Alpha-L-fucosidase AlfC fucosyltransferase mutant E274A · 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 K0NB39
Elsewhere: RCSB PDB 6O1I · PDBe 6O1I · UniProt K0NB39

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