Structure of PDB 1ded Chain A

Receptor sequence

>1dedA (length=686) Species: 1410 (Bacillus sp. 1011) [Search protein sequence]

APDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFDGSCTNLRLYC
GGDWQGIINKINDGYLTGMGITAIWISQPVENIYSVINYSGVNNTAYHGY
WARDFKKTNPAYGTMQDFKNLIDTAHAHNIKVIIDFAPNHTSPASSDDPS
FAENGRLYDNGNLLGGYTNDTQNLFHHYGGTDFSTIENGIYKNLYDLADL
NHNNSSVDVYLKDAIKMWLDLGVDGIRVDAVKNMPFGWQKSFMATINNYK
PVFTFGEWFLGVNEISPEYHQFANESGMSLLDFRFAQKARQVFRDNTDNM
YGLKAMLEGSEVDYAQVNDQVTFIDNHDMERFHTSNGDRRKLEQALAFTL
TSRGVPAIYYGSEQYMSGGNDPDNRARLPSFSTTTTAYQVIQKLAPLRKS
NPAIAYGSTHERWINNDVIIYERKFGNNVAVVAINRNMNTPASITGLVTS
LPRGSYNDVLGGILNGNTLTVGAGGAASNFTLAPGGTAVWQYTTDATTPI
IGNVGPMMAKPGVTITIDGRGFGSGKGTVYFGTTAVTGADIVAWEDTQIQ
VKIPAVPGGIYDIRVANAAGAASNIYDNFEVLTGDQVTVRFVINNATTAL
GQNVFLTGNVSELGNWDPNNAIGPMYNQVVYQYPTWYYDVSVPAGQTIEF
KFLKKQGSTVTWEGGANRTFTTPTSGTATVNVNWQP

3D structure

PDB

1ded Crystal structure of alkalophilic asparagine 233-replaced cyclodextrin glucanotransferase complexed with an inhibitor, acarbose, at 2.0 A resolution.

Chain

Resolution

2.0 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	D135 R227 D229 E257 H327 D328
Catalytic site (residue number reindexed from 1)	D135 R227 D229 E257 H327 D328
Enzyme Commision number	2.4.1.19: cyclomaltodextrin glucanotransferase.

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)
BS01	GLC	A	L194 Y195 N233 E257	L194 Y195 N233 E257
BS02	AC1	A	H98 Y100 W101 L197 D229 H327 D328 D371 R375	H98 Y100 W101 L197 D229 H327 D328 D371 R375
BS03	BGC	A	W616 K651 W662 N667	W616 K651 W662 N667
BS04	AC1	A	W662 E663 G664 P686	W662 E663 G664 P686
BS05	CA	A	D27 N29 N32 N33 G51 D53	D27 N29 N32 N33 G51 D53
BS06	CA	A	N139 I190 D199 N233	N139 I190 D199 N233

Gene Ontology

	Molecular Function
GO:0003824	catalytic activity
GO:0004556	alpha-amylase activity
GO:0016757	glycosyltransferase activity
GO:0030246	carbohydrate binding
GO:0043169	cation binding
GO:0043895	cyclomaltodextrin glucanotransferase activity
GO:0046872	metal ion binding
GO:2001070	starch binding

	Biological Process
GO:0005975	carbohydrate metabolic process

	Cellular Component
GO:0005576	extracellular region

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:1ded, PDBe:1ded, PDBj:1ded
PDBsum	1ded
PubMed	10731709
UniProt	P05618\|CDGT_BACS0 Cyclomaltodextrin glucanotransferase (Gene Name=cgt)

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