Structure of PDB 1lq2 Chain A

Receptor sequence
>1lq2A (length=602) Species: 4513 (Hordeum vulgare) [Search protein sequence]
DYVLYKDATKPVEDRVADLLGRMTLAEKIGQMTQIERLVATPDVLRDNFI
GSLLSGGGSVPRKGATAKEWQDMVDGFQKACMSTRLGIPMIYGIDAVHGQ
NNVYGATIFPHNVGLGATRDPYLVKRIGEATALEVRATGIQYAFAPCIAV
CRDPRWGRCYESYSEDRRIVQSMTELIPGLQGDVPKDFTSGMPFVAGKNK
VAACAKHFVGDGGTVDGINENNTIINREGLMNIHMPAYKNAMDKGVSTVM
ISYSSWNGVKMHANQDLVTGYLKDTLKFKGFVISDWEGIDRITTPAGSDY
SYSVKASILAGLDMIMVPNKYQQFISILTGHVNGGVIPMSRIDDAVTRIL
RVKFTMGLFENPYADPAMAEQLGKQEHRDLAREAARKSLVLLKNGKTSTD
APLLPLPKKAPKILVAGSHADNLGYQCGGWTIEWQGDTGRTTVGTTILEA
VKAAVDPSTVVVFAENPDAEFVKSGGFSYAIVAVGEHPYTETKGDNLNLT
IPEPGLSTVQAVCGGVRCATVLISGRPVVVQPLLAASDALVAAWLPGSEG
QGVTDALFGDFGFTGRLPRTWFKSVDQLPMNVGDAHYDPLFRLGYGLTTN
AT
3D structure
PDB1lq2 Three-dimensional Structure of the Barley {beta}-D-Glucan Glucohydrolase in Complex with a Transition State Mimic.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 IDD A D95 R158 K206 H207 M250 D285 W286 W434 E491 D95 R158 K206 H207 M250 D285 W286 W434 E491 PDBbind-CN: -logKd/Ki=8.77,Ki=1.7nM
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1lq2, PDBe:1lq2, PDBj:1lq2
PDBsum1lq2
PubMed14597633
UniProtQ9XEI3

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