Structure of PDB 5o8l Chain A

Receptor sequence
>5o8lA (length=1098) Species: 33964 (Leuconostoc citreum) [Search protein sequence]
AKGFDEQGNQIKIATDLSGNVYYFDASGKMLTGVQNIDGKKYYFDEQGHR
RRNYAGVFNNEFIYFGLDGVGQSAIEYQFEKGLTSQNSVATSHNAAKSYD
TKSFTNVDGFLTANSWYRPTDILRNGTKWEPSTETDFRPLLMTWWPDKEV
QANYLNYMSALGLGDQKIYTGASSQLDLNNAALIVQEAIEKKISLEKSTK
WLDDSIKSFIKSKRKDIQGNLVDTNPGWTIDSETGSTNHLQNGAFIFTNS
PLVPEANAAEGNRLINRTPSQQTGNHISYASQPYSGDDWGYELLLGNDVD
NSNPIVQAEQLNWIHYLMNFGTITAPQDPDAHLANFDSIRIDAVDNVDAD
LLQIAGDYFKAAYQVGENDKNANQHIHILQDWSPNDVWYNQQVNGNSQLT
MDATMQNQLLASLTRPITSRDSMKSFTKDALLVHRTADNSYNQAVPNYSF
IRAHDSEVQTIIAKIISDKHPDLYPTVDKALLAKDSALYDEAFTEYNADM
QKISSQKQYTHNNMPSAYAILLTNKDTVPRVYYGDLFTDNGEYMANKTPY
YDAITSLLTARTKFVSGGQSLSVDKNDVLTSVRYGKGALSATDNGSSDTR
NQGIGVIVSNNPNLDLNNDKVTLSMGISHAHQAYRPLLLTNSQGIVAYAT
DSEVPQNLYKTTNDKGELTFDASEIKGYDTVQTSGYLAVWVPVGASDEQD
ARTIASTEKNNGNSVYHSNAALDSQLIYEGFSNFQTVPSKNASADEYANV
IIAKHAADFNKWGVTSFQMAPQYRSSTDGSFLDAVDTVQNGYAFTDRYDL
GFNAADGSKNPTKYGTDEDLRNAIKSLHAQKTYDGSSIQVMADFVPDQLY
NMPLEQAVSVIRTDKYGVNSENPDIQNIIYAANIKSSGTDYQSIYGGKYL
AELQKNPLFKSLFDRIQISTKKTIDPNTRITQWSAKYFNGSNIQGKGINY
VLKDWASNKYFNVSSNDDMYSRLPKQLMNQESNTGFIVDDIGVKYYSISG
YQAKNTFVEDGNGEWYYFDNDGYMVKSTEESGPLRTVNASSKKYYILPNG
VEIRNSFGQDIQGNTYYFDARGEMVTSQYISDDTQNIYYFNNDGTMAK
3D structure
PDB5o8l Investigations on the Determinants Responsible for Low Molar Mass Dextran Formation by DSR-M Dextransucrase
ChainA
Resolution3.6 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 2.4.1.5: dextransucrase.
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 D677 H789 D790 D1118 Y1127 Q1183 D342 H454 D455 D783 Y792 Q848
BS02 FRU A Q715 D790 Q794 Q380 D455 Q459
BS03 CA A E627 D633 N681 D1182 E292 D298 N346 D847
Gene Ontology
Molecular Function
GO:0016757 glycosyltransferase activity
GO:0046527 glucosyltransferase activity
GO:0046872 metal ion binding
GO:0047849 dextransucrase activity
Biological Process
GO:0009250 glucan biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5o8l, PDBe:5o8l, PDBj:5o8l
PDBsum5o8l
PubMed
UniProtA0A2H4A2Q1

[Back to BioLiP]