MolNFT v1 · #120143 · protein

Crystal structure of branching enzyme from cyanothece sp. atcc 51142 in complex with maltoheptaose

5GQY · 1,4-alpha-glucan branching enzyme glgb: “Crystal structure of branching enzyme from cyanothece sp. atcc 51142 in complex with maltoheptaose”. X-ray diffraction, 2 ligands (GLC, MG), 6 pockets (best druggability 0.70). MolNFT v1…

PDB: 5GQY
Type: protein
Length: 755 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 1,4-alpha-glucan branching enzyme glgb
EC: 2.4.1.18
UniProt: B1WPM8
Ligands: GLC, MG
Pockets: 6 · best druggability 0.70

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	1,4-alpha-glucan branching enzyme glgb (EC 2.4.1.18)	protein	755	28% helix, 28% strand	B1WPM8

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 32 copies · chains A
MG · Magnesium ion · metal · 3 copies · chains A
GOL · Glycerol · additive · 2 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	548	0.70	0.79	49	empty
2	240	0.62	0.81	29	empty
3	129	0.53	0.81	23	empty
4	190	0.49	0.76	32	MG
5	132	0.37	0.73	21	GLC

Compared structures

5GQY · Crystal structure of branching enzyme from Cyanothece sp. ATCC 51142 in complex with… · 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 B1WPM8
Elsewhere: RCSB PDB 5GQY · PDBe 5GQY · UniProt B1WPM8

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