Structure of PDB 5hxm Chain A Binding Site BS04

Receptor Information
>5hxm Chain A (length=1060) Species: 1639 (Listeria monocytogenes) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MDGEYHSPYGDDDLYTVQPTERSPRDPKAGEDVILNITTWPIENGQDVWV
EWTKNGVAQENVTAAYDYNSGNNTYWKADLGKFEKGDEITYTTKGSTNGG
TAYESGPFTFYVTDWEYVQDVTSVVDNGDSITLNMTATAGDFSPKLYLSF
EDLDTLRMELSPTGKETGHAGKSGYTVEDTAEKVTVTTEDLSIEIQKSPY
RMEVHQADGTLLTSEYTTANSLGWLTDGKNVINQYQNNFMTPSDEAFYGF
GERYDTINQRGKDVETYVYNEYQDQAQTERTYLAVPFFVSANKYGMYVNS
DFHSQFQMASKVEDKYSFVLDNDGDMTNMLDYYVISGKDQNDIVNNYTDI
TGKTTLLPKWAFGLWMSANEWDRESDVSSALSNAKANDIPATGFVLEQWS
DEETYYIWNNATYTAKKNGEAFSYDDFTFNGKWTDPKGMVDSVHDAGMNI
VLWQVPVLKDDGTVYEQRDNDEEYMISQGYSADDGTGAPYRVPASQWFGN
GILLDFTNKDAVDWWTSQREYLLTEVGIDGFKTDGGEMVWGRDTTFSNGE
KGQEMRNRYPTDYVSSYFDFAKSINPEAVSFSRSGTSGAQKSGIYWSGDQ
TSTFDSFQASLKAGLSASTSGVSYWAWDMAGFTGDYPTAELYKRATAMAA
FAPIMQFHSEKSDPSPSEERSPWNAVARTGDETILPTFQKYLYTRMNLLP
YIYTAAKDTADNGKSMMRQMAMDYPEDVNARDLDEQYMFGDDLLVAPIVQ
EGQTEKEVYLPEGEWVDIWNGGVHPGGETISYYADVDTLPVFAKAGAIIP
MNMTDGYQLGQNVGNDLKSYDNLTFRVYPSGDSEYSFYDDVNGGEMRDIS
VSEDFANEKVSVDLPAMADETTMQVFSTEPTSVTIDGADVAKADTLDAFN
EATTGYYYDTVQNLTYVKAAAKDAKQAIVLNGVNHAPYEAEFGHLTNVTT
ASDHAGYTGTGFVAGFDAEKEAVEFDIDAVDGASDYTMEVRYSAGVEDAT
RTVYINGKKQQITLPKTANWDTWNTVEVPVTLQAGNNQVVFDFEADDTAG
INFDHVVIKK
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain5hxm Chain A Residue 1102 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5hxm Transferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		E370 D372 D376
Binding residue
(residue number reindexed from 1)		E370 D372 D376
Annotation score4
Enzymatic activity
Enzyme Commision number 3.2.1.177: alpha-D-xyloside xylohydrolase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5hxm, PDBe:5hxm, PDBj:5hxm
PDBsum5hxm
PubMed28089449
UniProtQ8Y4J2

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