Structure of PDB 1ot2 Chain A

Receptor sequence

>1ot2A (length=686) Species: 1397 (Niallia circulans) [Search protein sequence]

APDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFDGTCTNLRLYC
GGDWQGIINKINDGYLTGMGVTAIWISQPVENIYSIINYSGVNNTAYHGY
WARDFKKTNPAYGTIADFQNLIAAAHAKNIKVIINFAPNHTSPASSDQPS
FAENGRLYDNGTLLGGYTNDTQNLFHHNGGTDFSTTENGIYKNLYDLADL
NHNNSTVDVYLKDAIKMWLDLGIDGIRMDAVKHMPFGWQKSFMAAVNNYK
PVFTFGEWFLGVNEVSPENHKFANESGMSLLDFRFAQKVRQVFRDNTDNM
YGLKAMLEGSAADYAQVDDQVTFIDNHDMERFHASNANRRKLEQALAFTL
TSRGVPAIYYGTEQYMSGGTDPDNRARIPSFSTSTTAYQVIQKLAPLRKS
NPAIAYGSTQERWINNDVLIYERKFGSNVAVVAVNRNLNAPASISGLVTS
LPQGSYNDVLGGLLNGNTLSVGSGGAASNFTLAAGGTAVWQYTAATATPT
IGHVGPMMAKPGVTITIDGRGFGSSKGTVYFGTTAVSGADITSWEDTQIK
VKIPAVAGGNYNIKVANAAGTASNVYDNFEVLSGDQVSVRFVVNNATTAL
GQNVYLTGSVSELGNWDPAKAIGPMYNQVVYQYPNWYYDVSVPAGKTIEF
KFLKKQGSTVTWEGGSNHTFTAPSSGTATINVNWQP

3D structure

PDB

1ot2 The fully conserved Asp residue in Conserved sequence region I of the alpha-amylase Family is crucial for the Catalytic Site Architecture and Activity

Chain

Resolution

2.1 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)	N135 R227 D229 E257 H327 D328
Catalytic site (residue number reindexed from 1)	N135 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	BGC	A	Y100 H140 D229 H327 D328	Y100 H140 D229 H327 D328
BS02	GLC	A	H98 Y100 W101 Y195 D371 R375	H98 Y100 W101 Y195 D371 R375
BS03	GLC	A	Y89 Y195	Y89 Y195
BS04	GLC	A	G180 N193 Y195	G180 N193 Y195
BS05	GLC	A	S145 S146 D147	S145 S146 D147
BS06	GLC	A	K651 W662	K651 W662
BS07	GLC	A	W616 W662 N667	W616 W662 N667
BS08	GLC	A	T598 A599 L600 Q628 Y633	T598 A599 L600 Q628 Y633
BS09	GLC	A	L600 G601 Q602 N603 N627	L600 G601 Q602 N603 N627
BS10	GLC	A	W413 I414	W413 I414
BS11	GLC	A	E411 R412 G446	E411 R412 G446
BS12	CA	A	A315 D577	A315 D577
BS13	GLC	A	V262 Q287 R290 D295 E330	V262 Q287 R290 D295 E330
BS14	CA	A	D27 N29 N32 N33 G51 D53	D27 N29 N32 N33 G51 D53
BS15	CA	A	N139 I190 D199 H233	N139 I190 D199 H233

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:1ot2, PDBe:1ot2, PDBj:1ot2
PDBsum	1ot2
PubMed	12706817
UniProt	P43379\|CDGT2_NIACI Cyclomaltodextrin glucanotransferase (Gene Name=cgt)

[Back to BioLiP]