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The crystal structure of isomaltulose synthase mutant E295A from erwinia rhapontici NX5 in complex with D-glucose

Analyse The crystal structure of isomaltulose synthase mutant E295A from erwinia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HP5
Type: protein
Length: 559 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sucrose isomerase
EC: 5.4.99.11
UniProt: D9MPF2
Ligands: GLC, CA
Pockets: 7 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sucrose isomerase (EC 5.4.99.11)	protein	559	33% helix, 18% strand	D9MPF2

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · chains A
CA · Calcium ion · metal · chains A
GOL · Glycerol · additive · 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	129	0.80	0.97	26	GOL, GLC
2	193	0.56	0.79	21	empty
3	92	0.41	0.78	22	empty
4	73	0.36	0.77	19	empty
5	58	0.35	0.78	17	empty

Compared structures

4HP5 · The crystal structure of isomaltulose synthase mutant E295A from Erwinia rhapontici NX5… · 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 D9MPF2
Elsewhere: RCSB PDB 4HP5 · PDBe 4HP5 · UniProt D9MPF2

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