Structure of PDB 7vl2 Chain A

Receptor sequence
>7vl2A (length=706) Species: 945713 (Ignavibacterium album JCM 16511) [Search protein sequence]
SEKYFVKNGQPHFLISGEVHYFRINPKLWRNHLQLLKQTGADTVSTYIPW
DWHEIEEDDFDFEGKTHPARNLIRFIKLCKEENLDLIVKPGPYILAEYEN
QGLPSWLLKKLSKNAFALDENGNVISPDLVSYLSDEFLEYTFKWYDKVMP
IISKHQKEHYGPITMMQLCNEIGVFQWLSGKSDYNPKVINLYKEFIIQRY
KTIEKLNSVYSTNYNSFDDLKAPSGKIKLRSDYCAYFDFHLFFREYYNKY
ISILKNKIRSFGINIKLTHNIPGWIYGNASELPMLISTYSEIMKNHPDII
FGLDHIPEFVSFRNAHSDLACNKILEAMQPEAPVWAAEFQAGTREHHVKA
YAKDLETFYIASLAHGIKGFNYYMFSQGINPEGKGFYGKTFYFQTALDAA
SNKLALYDSIKKVNRFIRKEQKDLLRTNVNSEICVGFYKPYFFTELISSQ
LLKEKKLNVEELGLYIDPRFLREEILFNGLLRGLQTLNYNYDVVDLENCD
LKSLTAYKQLWITSAEFMDAETQNLLSEFVLNGGNLILYPAVPTLDNYLN
RCEILKNNFGIEFITKDSSHKVSAFGIEDVFTAFSKKQIYNDTNSKPIAF
TQENEICGIRKKIGKGELTILGFAFGYTSDEHLELIDKLVKLNKIKRELF
VSDKDIQFVVRENNKSRYIFFLNYHNERKTFNYRKSSKSEEISIAPFSYK
VIKENK
3D structure
PDB7vl2 Characterization and structural analyses of a novel glycosyltransferase acting on the beta-1,2-glucosidic linkages.
ChainA
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 BW3 A E176 W182 L183 G278 W279 I280 R349 E171 W177 L178 G273 W274 I275 R344
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005773 vacuole

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7vl2, PDBe:7vl2, PDBj:7vl2
PDBsum7vl2
PubMed35065074
UniProtI0AIT9

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