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Crystal structure of branching enzyme Y500A mutant from cyanothece sp. atcc 51142

Analyse Crystal structure of branching enzyme Y500A mutant from cyanothece sp. atcc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GQZ
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: MG
Pockets: 6 · best druggability 0.71

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

MG · Magnesium ion · metal · 4 copies · chains A
GOL · Glycerol · additive · 9 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	557	0.71	0.80	48	empty
2	236	0.64	0.82	28	empty
3	195	0.49	0.76	32	MG
4	119	0.47	0.79	21	empty
5	62	0.37	0.79	16	empty

Compared structures

5GQZ · Crystal structure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142 · 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 5GQZ · PDBe 5GQZ · UniProt B1WPM8

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