Structure of PDB 1eo5 Chain A

Receptor sequence

>1eo5A (length=686) Species: 1397 (Niallia circulans) [Search protein sequence]

APDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFDGTCTNLRLYC
GGDWQGIINKINDGYLTGMGVTAIWISQPVENIYSIINYSGVNNTAYHGY
WARDFKKTNPAYGTIADFQNLIAAAHAKNIKVIIDFAPNHTSPASSDQPS
FAENGRLYDNGTLLGGYTNDTQNLFHHNGGTDFSTTENGIYKNLYDLADL
NHNNSTVDVYLKDAIKMWLDLGIDGIRMAAVKHMPFGWQKSFMAAVNNYK
PVFTFGAWFLGVNEVSPENHKFANESGMSLLDFRFAQKVRQVFRDNTDNM
YGLKAMLEGSAADYAQVDDQVTFIDNHDMERFHASNANRRKLEQALAFTL
TSRGVPAIYYGTEQYMSGGTDPDNRARIPSFSTSTTAYQVIQKLAPLRKS
NPAIAYGSTQERWINNDVLIYERKFGSNVAVVAVNRNLNAPASISGLVTS
LPQGSYNDVLGGLLNGNTLSVGSGGAASNFTLAAGGTAVWQYTAATATPT
IGHVGPMMAKPGVTITIDGRGFGSSKGTVYFGTTAVSGADITSWEDTQIK
VKIPAVAGGNYNIKVANAAGTASNVYDNFEVLSGDQVSVRFVVNNATTAL
GQNVYLTGSVSELGNWDPAKAIGPMYNQVVYQYPNWYYDVSVPAGKTIEF
KFLKKQGSTVTWEGGSNHTFTAPSSGTATINVNWQP

3D structure

PDB

1eo5 Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity.

Chain

Resolution

2.0 Å

3D
structure

Catalytic site residues are labeled in the 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

Catalytic site (original residue number in PDB)	D135 R227 A229 A257 H327 D328
Catalytic site (residue number reindexed from 1)	D135 R227 A229 A257 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	BGC	A	Y100 H140 R227 A229 H327 D328	Y100 H140 R227 A229 H327 D328
BS02	GLC	A	Y100 W101 Y195 D371 R375	Y100 W101 Y195 D371 R375
BS03	GLC	A	Y89 D371	Y89 D371
BS04	GLC	A	Y89 D196	Y89 D196
BS05	GLC	A	G180 N193 Y195	G180 N193 Y195
BS06	GLC	A	S145 S146 D147	S145 S146 D147
BS07	GLC	A	K651 W662	K651 W662
BS08	GLC	A	W616 W662 N667	W616 W662 N667
BS09	GLC	A	T598 A599 L600 Y633	T598 A599 L600 Y633
BS10	GLC	A	L600 G601 Q602 N603 N627 Q628	L600 G601 Q602 N603 N627 Q628
BS11	GLC	A	W413 I414	W413 I414
BS12	GLC	A	E411 R412 G446	E411 R412 G446
BS13	CA	A	D27 N29 N32 N33 G51 D53	D27 N29 N32 N33 G51 D53
BS14	CA	A	N139 I190 D199 H233	N139 I190 D199 H233
BS15	CA	A	A315 D577	A315 D577

Gene Ontology

	Molecular Function
GO:0003824	catalytic 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:1eo5, PDBe:1eo5, PDBj:1eo5
PDBsum	1eo5
PubMed	10869182
UniProt	P43379\|CDGT2_NIACI Cyclomaltodextrin glucanotransferase (Gene Name=cgt)

[Back to BioLiP]