Structure of PDB 2x2i Chain C

Receptor sequence

>2x2iC (length=1025) Species: 2782 (Gracilariopsis lemaneiformis) [Search protein sequence]

TDNPDGIDYKTYDYVGVWGFSPLSNTNWFAAGSSTPGGITDWTATMNVNF
DRIDNPSITVQHPVQVQVTSYNNNSYRVRFNPDGPIRDVTRGPILKQQLD
WIRTQELSEGCDPGMTFTSEGFLTFETKDLSVIIYGNFKTRVTRKSDGKV
IMENDEVGTASSGNKCRGLMFVDRLYGNAIASVNKNFRNDAVKQEGFYGA
GEVNCKYQDTYILERTGIAMTNYNYDNLNYNQWDLRPPHHDGALNPDYYI
PMYYAAPWLIVNGCAGTSEQYSYGWFMDNVSQSYMNTGDTTWNSGQEDLA
YMGAQYGPFDQHFVYGAGGGMECVVTAFSLLQGKEFENQVLNKRSVMPPK
YVFGFFQGVFGTSSLLRAHMPAGENNISVEEIVEGYQNNNFPFEGLAVDV
DMQDNLRVFTTKGEFWTANRVGTGGDPNNRSVFEWAHDKGLVCQTNITCF
LRNDNEGQDYEVNQTLRERQLYTKNDSLTGTDFGMTDDGPSDAYIGHLDY
GGGVECDALFPDWGRPDVAEWWGNNYKKLFSIGLDFVWQDMTVPAMMPHK
IGDDINVKPDGNWPNADDPSNGQYNWKTYHPQVLVTDMRYENHGREPMVT
QRNIHAYTLCESTRKEGIVENADTLTKFRRSYIISRGGYIGNQHFGGMWV
GDNSTTSNYIQMMIANNINMNMSCLPLVGSDIGGFTSYDNENQRTPCTGD
LMVRYVQAGCLLPWFRNHYDRWIESKDHGKDYQELYMYPNEMDTLRKFVE
FRYRWQEVLYTAMYQNAAFGKPIIKAASMYNNDSNVRRAQNDHFLLGGHD
GYRILCAPVVWENSTERELYLPVLTQWYKFGPDFDTKPLEGAMNGGDRIY
NYPVPQSESPIFVREGAILPTRYTLNGENKSLNTYTDEDPLVFEVFPLGN
NRADGMCYLDDGGVTTNAEDNGKFSVVKVAAEQDGGTETITFTNDCYEYV
FGGPFYVRVRGAQSPSNIHVSSGAGSQDMKVSSATSRAALFNDGENGDFW
VDQETDSLWLKLPNVVLPDAVITIT

3D structure

PDB

2x2i Crystal Structure of Alpha-1,4-Glucan Lyase, a Unique Glycoside Hydrolase Family Member with a Novel Catalytic Mechanism.

Chain

Resolution

2.6 Å

3D
structure

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Enzymatic activity

Enzyme Commision number

4.2.2.13: exo-(1->4)-alpha-D-glucan lyase.

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	GLC	C	L241 Q245 Y513 H741	L228 Q232 Y500 H728
BS02	AC1	C	D239 F373 D412 Y513 D553 M554 R649 D665 F698 H731	D226 F360 D399 Y500 D540 M541 R636 D652 F685 H718
BS03	AC1	C	T24 G32 F33 S34 S37 T39 N40 W41 V185 G190 N191 A192 Q318	T11 G19 F20 S21 S24 T26 N27 W28 V172 G177 N178 A179 Q305

Gene Ontology

	Molecular Function
GO:0003824	catalytic activity
GO:0004553	hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798	hydrolase activity, acting on glycosyl bonds
GO:0016829	lyase activity
GO:0030246	carbohydrate binding
GO:0047457	exo-(1,4)-alpha-D-glucan lyase activity

	Biological Process
GO:0005975	carbohydrate metabolic process

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Molecular Function

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Biological Process

External links

PDB	RCSB:2x2i, PDBe:2x2i, PDBj:2x2i
PDBsum	2x2i
PubMed	23902768
UniProt	Q9STC1

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