Structure of PDB 6hur Chain A

Receptor sequence
>6hurA (length=428) Species: 1682 (Bifidobacterium longum subsp. infantis) [Search protein sequence]
KSDVTAQDVENALTDTSKNVELTVWAYSAKQMEPTVKAFEKKYPHIKINF
VNTGAAEDHFTKFQNVVQAQKDIPDVVQMSANKFQQFAVSGALLNFANDS
IEKAWSKLYTKTAWAQVHYAGGLYGAPQDATPLANYVRKDILDEHNLQVP
ESWEDIYNEGIKLHKEDSNKYMGILGSDISFFTNLYRSVGARLWKVNSVD
DVELTMNSGKAKEFTEFLQKCLKDGVLEGGTVFTDEFNRSINDGRYATFI
NENWMGNTYKEQNPSLKGKMVVAAPPSWKGQPYQSSSVGSMMSVSAACPK
EKQAAALAFINWLDSDKDAIQSWQDTNNGNFFMAASVYQDDENQRNKKET
DGYYANDDVNAVYFDSMDKVNTDWEYLPFMSQVEVVFNDVIVPEMNENGD
LVGAMAKAQQKLKAYAEDNGFKVTTDAD
3D structure
PDB6hur Evolutionary adaptation in fucosyllactose uptake systems supports bifidobacteria-infant symbiosis.
ChainA
Resolution1.297 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 GLC A Y59 A88 Y27 A56
BS02 GAL A S60 Q63 D161 W286 S322 S28 Q31 D129 W254 S290
BS03 FUC A Y59 S112 K115 S212 E284 V320 G321 Y27 S80 K83 S180 E252 V288 G289
BS04 ZN A E134 H150 E102 H118
BS05 ZN A D348 D350 D316 D318
BS06 ZN A H177 D199 H145 D167
BS07 ZN A D267 E268 D235 E236
Gene Ontology
Molecular Function
GO:0046872 metal ion binding
GO:1901982 maltose binding
Biological Process
GO:0015768 maltose transport
GO:0042956 maltodextrin transmembrane transport
Cellular Component
GO:0055052 ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6hur, PDBe:6hur, PDBj:6hur
PDBsum6hur
PubMed31489370
UniProtA0A1S2VYK0

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