Structure of PDB 5dze Chain A

Receptor sequence
>5dzeA (length=199) Species: 29760 (Vitis vinifera) [Search protein sequence]
EAQPLKFIAVDYCPESCTHSPESSTITLTFDHRGGSRWRSTTRFQYGTFS
SLIQCPKGNTSGLNFNIYLSSLEGDKSQDAIDFEFLGKDKRIVQTNYYTA
GTGNREAIHDLGFDCSDGFHEYVIKWGPDLIQWLIDGKVIRSVRADGEGF
PQKPMFLYASVWDASYIDEGRWTGPYVGCDAPYICLYKNVNVPVGTAVE
3D structure
PDB5dze Crystallographic insight into the evolutionary origins of xyloglucan endotransglycosylases and endohydrolases.
ChainA
Resolution0.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A89 D91 E93
Catalytic site (residue number reindexed from 1) A80 D82 E84
Enzyme Commision number 3.2.1.73: licheninase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GLC A N75 Y77 E82 D91 E93 W171 N66 Y68 E73 D82 E84 W162
BS02 BGC A Y21 R46 Y77 S169 W171 Y12 R37 Y68 S160 W162
BS03 BGC A Y21 R46 Y12 R37
BS04 BGC A E93 Y107 E115 W181 E84 Y98 E106 W172
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5dze, PDBe:5dze, PDBj:5dze
PDBsum5dze
PubMed27859885
UniProtF6I323

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