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Crystal structure of branching enzyme W610A mutant from cyanothece sp. atcc 51142

Analyse Crystal structure of branching enzyme W610A 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: 5GR5
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: 7 · 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

MG · Magnesium ion · metal · 3 copies · chains A
GOL · Glycerol · additive · 4 copies · chains A

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

Pockets

7 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	553	0.70	0.79	48	empty
2	242	0.63	0.81	31	empty
3	101	0.48	0.80	18	empty
4	145	0.45	0.76	29	empty
5	88	0.38	0.76	17	empty

Compared structures

5GR5 · Crystal structure of branching enzyme W610A 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 5GR5 · PDBe 5GR5 · UniProt B1WPM8

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