Structure of PDB 6mi1 Chain A

Receptor sequence
>6mi1A (length=606) Species: 112509 (Hordeum vulgare subsp. vulgare) [Search protein sequence]
HHAADYVLYKDATKPVEDRVADLLGRMTLAEKIGQMTQIERLVATPDVLR
DNFIGSLLSGGGSVPRKGATAKEWQDMVDGFQKACMSTRLGIPMIYGIDA
VHGQNNVYGATIFPHNVGLGATRDPYLVKRIGEATALEVRATGIQYAFAP
CIAVCRDPRWGACYASYSEDRRIVQSMTELIPGLQGDVPKDFTSGMPFVA
GKNKVAACAKHFVGDGGTVDGINENNTIINREGLMNIHMPAYKNAMDKGV
STVMISYSSWNGVKMHANQDLVTGYLKDTLKFKGFVISDWEGIDRITTPA
GSDYSYSVKASILAGLDMIMVPNKYQQFISILTGHVNGGVIPMSRIDDAV
TRILRVKFTMGLFENPYADPAMAEQLGKQEHRDLAREAARKSLVLLKNGK
TSTDAPLLPLPKKAPKILVAGSHADNLGYQCGGWTIEWQGDTGRTTVGTT
ILEAVKAAVDPSTVVVFAENPDAEFVKSGGFSYAIVAVGEHPYTETKGDN
LNLTIPEPGLSTVQAVCGGVRCATVLISGRPVVVQPLLAASDALVAAWLP
GSEGQGVTDALFGDFGFTGRLPRTWFKSVDQLPMNVGDAHYDPLFRLGYG
LTTNAT
3D structure
PDB6mi1 Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site.
ChainA
Resolution2.3 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) D289 E495
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 U1Y A G56 G57 W286 W434 G60 G61 W290 W438
BS02 BGC A D95 K206 H207 D285 E491 D99 K210 H211 D289 E495
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6mi1, PDBe:6mi1, PDBj:6mi1
PDBsum6mi1
PubMed31110237
UniProtQ9XEI3

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