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Cycloalternan-degrading enzyme from trueperella pyogenes in complex with isomaltose

Analyse Cycloalternan-degrading enzyme from trueperella pyogenes in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5I0E
Type: protein
Length: 703 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase family 31
UniProt: X4QP62
Ligands: GLC, CA
Pockets: 6 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Glycoside hydrolase family 31	protein	703	24% helix, 28% strand	X4QP62

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 2 copies · chains B
CA · Calcium ion · metal · 3 copies · chains B
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains B

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	588	0.74	0.81	50	empty
2	278	0.60	0.78	32	GLC
3	75	0.38	0.78	18	empty
4	61	0.36	0.79	18	empty
5	74	0.29	0.73	21	empty

Compared structures

5I0E · Cycloalternan-degrading enzyme from Trueperella pyogenes in complex with isomaltose · the same entry in another collection · chain B against B, 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 X4QP62
Elsewhere: RCSB PDB 5I0E · PDBe 5I0E · UniProt X4QP62

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