Structure of PDB 3wlp Chain A

Receptor sequence

>3wlpA (length=602) Species: 112509 (Hordeum vulgare subsp. vulgare)

DYVLYKDATKPVEDRVADLLGRMTLAEKIGQMTQIERLVATPDVLRDNFI
GSLLSGGGSVPRKGATAKEWQDMVDGFQKACMSTRLGIPMIYGIDAVHGQ
NNVYGATIFPHNVGLGATRDPYLVKRIGEATALEVRATGIQYAFAPCIAV
CRDPRWGRCYESYSEDRRIVQSMTELIPGLQGDVPKDFTSGMPFVAGKNK
VAACAKHFVGDGGTVDGINENNTIINREGLMNIHMPAYKNAMDKGVSTVM
ISYSSWNGVKMHANQDLVTGYLKDTLKFKGFVISDWEGIDRITTPAGSDY
SYSVKASILAGLDMIMVPNKYQQFISILTGHVNGGVIPMSRIDDAVTRIL
RVKFTMGLFENPYADPAMAEQLGKQEHRDLAREAARKSLVLLKNGKTSTD
APLLPLPKKAPKILVAGSHADNLGYQCGGWTIEWQGDTGRTTVGTTILEA
VKAAVDPSTVVVFAENPDAEFVKSGGFSYAIVAVGEHPYTETKGDNLNLT
IPEPGLSTVQAVCGGVRCATVLISGRPVVVQPLLAASDALVAAWLPGSEG
QGVTDALFGDFGFTGRLPRTWFKSVDQLPMNVGDAHYDPLFRLGYGLTTN
AT

3D structure

• PDB: 3wlp Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site.
• Chain: A
• Resolution: 1.57 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D285 E491
• Catalytic site (residue number reindexed from 1): D285 E491
• Enzyme Commision number: 3.2.1.21: beta-glucosidase.

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	MGL	A	G56 G57 W286 W434	G56 G57 W286 W434
BS02	GS1	A	D95 R158 K206 H207 M250 D285 W286	D95 R158 K206 H207 M250 D285 W286

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

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:3wlp, PDBe:3wlp, PDBj:3wlp
• PDBsum: 3wlp
• PubMed: 31110237
• UniProt: Q9XEI3