Structure of PDB 1ua3 Chain A

Receptor sequence

>1ua3A (length=496) Species: 9823 (Sus scrofa) [Search protein sequence]

QYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIV
VTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVIN
HMCGSGAAAGTGTTCGSYCNPGNREFPAVPYSAWDFNDGKCKTASGGIES
YNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASK
HMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAIKSSEYFGN
GRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHD
NQRGHGAGGSSILTFWDARLYKIAVGFMLAHPYGFTRVMSSYRWARNFVN
GEDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWREIRNMVWFRNV
VDGQPFANWWDNGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYC
DVISGDKVGNSCTGIKVYVSSDGTAQFSISNSAEDPFIAIHAESKL

3D structure

PDB

1ua3 Crystal Structure of the Pig Pancreatic alpha-Amylase Complexed with Malto-Oligosaccharides

Chain

Resolution

2.01 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	D197 S226 D300
Catalytic site (residue number reindexed from 1)	D197 S226 D300
Enzyme Commision number	3.2.1.1: alpha-amylase.

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	A318 K322 T377 W388 E390	A318 K322 T377 W388 E390
BS02	GLC	A	T376 R387 R389 E390	T376 R387 R389 E390
BS03	GLC	A	Y62 H101 R195 D197 E233 H299 D300	Y62 H101 R195 D197 E233 H299 D300
BS04	GLC	A	W58 W59 Q63	W58 W59 Q63
BS05	GLC	A	W59 V163	W59 V163
BS06	GLC	A	E272 Y276 N279 W284	E272 Y276 N279 W284
BS07	GLC	A	K261 G283 W284	K261 G283 W284
BS08	CL	A	R195 R337	R195 R337
BS09	CA	A	N100 R158 D167 H201	N100 R158 D167 H201
BS10	BGC	A	K140 W203 D206	K140 W203 D206
BS11	EDO	A	S132 D135 Y174	S132 D135 Y174
BS12	EDO	A	K172 Y174	K172 Y174
BS13	EDO	A	R30 T376 R387	R30 T376 R387

Gene Ontology

	Molecular Function
GO:0003824	catalytic activity
GO:0004556	alpha-amylase activity
GO:0005509	calcium ion binding
GO:0016160	amylase activity
GO:0016798	hydrolase activity, acting on glycosyl bonds
GO:0031404	chloride ion binding
GO:0043169	cation binding
GO:0046872	metal ion binding

	Biological Process
GO:0005975	carbohydrate metabolic process
GO:0016052	carbohydrate catabolic process

	Cellular Component
GO:0005576	extracellular region
GO:0005615	extracellular space

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:1ua3, PDBe:1ua3, PDBj:1ua3
PDBsum	1ua3
PubMed	12962327
UniProt	P00690\|AMYP_PIG Pancreatic alpha-amylase (Gene Name=AMY2)

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