Structure of PDB 1kcl Chain A

Receptor sequence

>1kclA (length=686) Species: 1397 (Niallia circulans) [Search protein sequence]

APDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFDGTCTNLRLYC
GGDWQGIINKINDGYLTGMGVTAIWISQPVENIYSIINYSGVNNTAYHGY
WARDFKKTNPAYGTIADFQNLIAAAHAKNIKVIIDFAPNHTSPASSDQPS
FAENGRLYDNGTLLGGYTNDTQNLFHHNLGTDFSTTENGIYKNLYDLADL
NHNNSTVDVYLKDAIKMWLDLGIDGIRMDAVKHMPFGWQKSFMAAVNNYK
PVFTFGEWFLGVNEVSPENHKFANESGMSLLDFRFAQKVRQVFRDNTDNM
YGLKAMLEGSAADYAQVDDQVTFIDNHDMERFHASNANRRKLEQALAFTL
TSRGVPAIYYGTEQYMSGGTDPDNRARIPSFSTSTTAYQVIQKLAPLRKC
NPAIAYGSTQERWINNDVLIYERKFGSNVAVVAVNRNLNAPASISGLVTS
LPQGSYNDVLGGLLNGNTLSVGSGGAASNFTLAAGGTAVWQYTAATATPT
IGHVGPMMAKPGVTITIDGRGFGSSKGTVYFGTTAVSGADITSWEDTQIK
VKIPAVAGGNYNIKVANAAGTASNVYDNFEVLSGDQVSVRFVVNNATTAL
GQNVYLTGSVSELGNWDPAKAIGPMYNQVVYQYPNWYYDVSVPAGKTIEF
KFLKKQGSTVTWEGGSNHTFTAPSSGTATINVNWQP

3D structure

PDB

1kcl The remote substrate binding subsite -6 in cyclodextrin-glycosyltransferase controls the transferase activity of the enzyme via an induced-fit mechanism.

Chain

Resolution

1.94 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	F183 F259	F183 F259
BS02	GLC	A	Y195 H233 E257	Y195 H233 E257
BS03	GLC	A	Y100 H140 D229 E257 H327 D328	Y100 H140 D229 E257 H327 D328
BS04	BGC	A	D371 R375	D371 R375
BS05	GLC	A	K651 W662	K651 W662
BS06	GLC	A	W616 W662 N667	W616 W662 N667
BS07	GLC	A	W413 I414	W413 I414
BS08	GLC	A	E411 R412 G446	E411 R412 G446
BS09	GLC	A	T598 A599 L600 Y633	T598 A599 L600 Y633
BS10	GLC	A	G601 Q602 N603 N627	G601 Q602 N603 N627
BS11	CA	A	D27 N29 N32 N33 G51 D53	D27 N29 N32 N33 G51 D53
BS12	CA	A	N139 I190 D199 H233	N139 I190 D199 H233
BS13	GLC	A	V262 R290 D295 E330	V262 R290 D295 E330

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

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:1kcl, PDBe:1kcl, PDBj:1kcl
PDBsum	1kcl
PubMed	11696539
UniProt	P43379\|CDGT2_NIACI Cyclomaltodextrin glucanotransferase (Gene Name=cgt)

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