Structure of PDB 1ug9 Chain A

Receptor sequence

>1ug9A (length=1019) Species: 1665 (Arthrobacter globiformis) [Search protein sequence]

TAEPPGSPGAAATWTKGDKEGVGTSLNPASKVWYTLTEGTMSEVYYPHAD
TPNTRELQFAVSDGTSAQRESEQTTRTVELADPKALSYRQTTTDNAGRWR
LTKTYVTDPRRSTVMLGVTFEVLDGGDYQLFVLSDPSLAGTSGGDTGSVT
DGALLASDLADAATPVATALVSSVGFGAVANGYVGTSDGWTDLAADGRLD
NASATAGPGNISQTGQIPLAAGGKTEFSLALGFGADTAEALATAKASLGT
GYKKVSKSYTGEWKKYLNSLDAPATSLTGALRTQYDVSLMTVKSHEDKTF
PGAFIASLTIPWGQAASAETHREGYHAVWARDMYQSVTALLAAGDEEAAA
RGVEWLFTYQQQPDGHFPQTSRVDGTIGQNGIQLDETAFPILLANQIGRT
DAGFYRNELKPAADYLVAAGPKTPQERWEETGGYSTSTLASQIAALAAAA
DIAGKNGDAGSAAVYRATADEWQRSTEKWMFTTNGPVGDGKYYLRISATG
NPNDGATRDWGNGAGVHPENAVLDGGFLEFVRLGVKAPADPYVADSLAET
DASISQETPGGRMWHRYTYDGYGEKADGSPWDGTGIGRLWPLLSGERGEY
ALANGQDALPYLETMHSAANAGYMIPEQVWDRDEPTSYGHELGRSTGSAS
PLSWAMAQYVRLAAGVKAGAPVETPQNVAARYAAGTPLSSPELSVTAPEA
LSTADSATAVVRGTTNAAKVYVSVNGTATEAPVTDGTFSLDVALTGAKNK
VTVAAVAADGGTAVEDRTVLYYGSRIGALSDPAGDDNGPGTYRYPTNSAY
VPGAFDLTGVDVYDAGDDYAFVATIAGEVTNPWGGQAISHQRVNIYLGKG
EGGATPGLPGTNINLEHAWDSVIVTDGRFDGAGVYAPDGTRTSAVSLLAV
PEARQIVTRVPKAALGGLDPATARMSVAMFGNAESGEGIGNVRPVYDGAY
WEAGDPAWIKEWRFGGGAGVFDGTIPSRDTDTDDPNALDVLVGEGQTQAA
VLDWRAGSPVVVPMLGLQP

3D structure

PDB

1ug9 Structural insights into substrate specificity and function of glucodextranase

Chain

Resolution

2.5 Å

3D
structure

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Enzymatic activity

Enzyme Commision number

3.2.1.70: glucan 1,6-alpha-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	CA	A	L139 T142 G144 D146 D159	L138 T141 G143 D145 D158
BS02	CA	A	F358 Q362 E409	F357 Q361 E408
BS03	CA	A	D136 P137 N211 I212	D135 P136 N210 I211
BS04	CA	A	V946 A969 D980 D982 D985	V945 A968 D979 D981 D984
BS05	CA	A	D782 P783 D786 D807 L808 D990	D781 P782 D785 D806 L807 D989
BS06	CA	A	D782 D786 D990 V991 Q999	D781 D785 D989 V990 Q998

Gene Ontology

	Molecular Function
GO:0003824	catalytic activity
GO:0004339	glucan 1,4-alpha-glucosidase activity
GO:0004553	hydrolase activity, hydrolyzing O-glycosyl compounds
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:1ug9, PDBe:1ug9, PDBj:1ug9
PDBsum	1ug9
PubMed	14660574
UniProt	Q9LBQ9

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