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Crystal structure of BHGH81 mutant in complex with laminaro-hexaose

Analyse Crystal structure of BHGH81 mutant in complex with laminaro-hexaose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5T4C
Type: protein
Length: 752 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase
UniProt: Q9KG76
Ligands: BGC, PO4
Pockets: 6 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase	protein	752	28% helix, 26% strand	Q9KG76

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 11 copies · chains A
PO4 · Phosphate ion · ion · 10 copies · chains A
EDO · 1,2-ethanediol · additive · 12 copies · chains A

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	93	0.69	0.93	22	empty
2	178	0.60	0.82	28	BGC
3	178	0.54	0.79	33	EDO
4	98	0.50	0.82	26	empty
5	101	0.42	0.77	18	PO4

Compared structures

5T4C · Crystal structure of BhGH81 mutant in complex with laminaro-hexaose · 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 Q9KG76
Elsewhere: RCSB PDB 5T4C · PDBe 5T4C · UniProt Q9KG76

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