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The crystal structure of isomaltulose synthase from erwinia rhapontici NX5 in complex with tris

Analyse The crystal structure of isomaltulose synthase from erwinia rhapontici NX5 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HOX
Type: protein
Length: 558 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: CA
Pockets: 8 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sucrose isomerase (EC 5.4.99.11)	protein	558	35% helix, 18% strand	D9MPF2

Ligands and binding sites

CA · Calcium ion · metal · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
GOL · Glycerol · additive · chains A

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

Pockets

8 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	82	0.73	0.97	23	TRS, GOL
2	194	0.58	0.81	20	empty
3	74	0.36	0.77	21	empty
4	60	0.35	0.77	12	empty
5	64	0.33	0.76	17	empty

Compared structures

4HOX · The crystal structure of isomaltulose synthase from Erwinia rhapontici NX5 in complex… · the same entry in another collection · chain A against A, TM-score 1.00

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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 4HOX · PDBe 4HOX · UniProt D9MPF2

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