Structure of PDB 2d0h Chain A

Receptor sequence

>2d0hA (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

2d0h 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

2.1 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 Y360 Q396 W398	F310 Y360 Q396 W398
BS03	GLC	A	Y223 H267 F310 N356 Q396 H471 D472	Y223 H267 F310 N356 Q396 H471 D472
BS04	GLC	A	H221 F313 D516 R520	H221 F313 D516 R520
BS05	GLC	A	F313 D516	F313 D516
BS06	CA	A	A2 D4 N6 D42 D96	A2 D4 N6 D42 D96
BS07	CA	A	N145 D147 N150 D151 G187 D189	N145 D147 N150 D151 G187 D189
BS08	CA	A	D276 N279 F281 S282 S283 E288	D276 N279 F281 S282 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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:2d0h, PDBe:2d0h, PDBj:2d0h
PDBsum	2d0h
PubMed	16302977
UniProt	Q60053\|NEPU1_THEVU Neopullulanase 1 (Gene Name=tvaI)

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