Structure of PDB 2d0g Chain A

Receptor sequence

>2d0gA (length=637) Species: 2026 (Thermoactinomyces vulgaris) [Search protein sequence]

AANDNNVEWNGLFHDQGPLFDNAPEPTSTQSVTLKLRTFKGDITSANIKY
WDTADNAFHWVPMVWDSNDPTGTFDYWKGTIPASPSIKYYRFQINDGTST
AWYNGNGPSSTEPNADDFYIIPNFKTPDWLKNGVMYQIFPDRFYNGDSSN
DVQTGSYTYNGTPTEKKAWGSSVYADPGYDNSLVFFGGDLAGIDQKLGYI
KKTLGANILYLNPIFKAPTNHKYDTQDYMAVDPAFGDNSTLQTLINDIHS
TANGPKGYLILDGVFNHTGDSHPWFDKYNNFSSQGAYESQSSPWYNYYTF
YTWPDSYASFLGFNSLPKLNYGNSGSAVRGVIYNNSNSVAKTYLNPPYSV
DGWRLNAAQYVDANGNNGSDVTNHQIWSEFRNAVKGVNSNAAIIGQYWGN
ANPWTAQGNQWDAATNFDGFTQPVSEWITGKDYQNNSASISTTQFDSWLR
GTRANYPTNVQQSMMNFLSNHDITRFATRSGGDLWKTYLALIFQMTYVGT
PTIYYGDEYGMQGGADPDNRRSFDWSQATPSNSAVALTQKLITIRNQYPA
LRTGSFMTLITDDTNKIYSYGRFDNVNRIAVVLNNDSVSHTVNVPVWQLS
MPNGSTVTDKITGHSYTVQNGMVTVAVDGHYGAVLAQ

3D structure

PDB

2d0g Complexes of Thermoactinomyces vulgaris R-47 alpha-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with alpha-(1,6) glycosidic linkages

Chain

Resolution

2.6 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	D262 R354 N356 Q396 H471 D472
Catalytic site (residue number reindexed from 1)	D262 R354 N356 Q396 H471 D472
Enzyme Commision number	3.2.1.135: neopullulanase.

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	W398 Q434 D472	W398 Q434 D472
BS02	GLC	A	F310 L311 Y360 Q396 W398	F310 L311 Y360 Q396 W398
BS03	GLC	A	Y223 H267 F310 N356 Q396 H471 D472	Y223 H267 F310 N356 Q396 H471 D472
BS04	GLC	A	H221 Y223 D516 R520	H221 Y223 D516 R520
BS05	BGC	A	Y174 A515	Y174 A515
BS06	BGC	A	Y89 D117	Y89 D117
BS07	BGC	A	A115 D116	A115 D116
BS08	BGC	A	K40 W65 N68	K40 W65 N68
BS09	BGC	A	G41 D75	G41 D75
BS10	GLC	A	D418 W448	D418 W448
BS11	BGC	A	W485 G629 H630	W485 G629 H630
BS12	CA	A	A2 D4 N6 D42 D96	A2 D4 N6 D42 D96
BS13	CA	A	N145 D147 N150 D151 G187 D189	N145 D147 N150 D151 G187 D189
BS14	CA	A	D276 N279 F281 S283 E288	D276 N279 F281 S283 E288

Gene Ontology

	Molecular Function
GO:0004553	hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798	hydrolase activity, acting on glycosyl bonds
GO:0031216	neopullulanase activity
GO:0046872	metal ion 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:2d0g, PDBe:2d0g, PDBj:2d0g
PDBsum	2d0g
PubMed	16302977
UniProt	Q60053\|NEPU1_THEVU Neopullulanase 1 (Gene Name=tvaI)

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