Structure of PDB 1xh1 Chain A

Receptor sequence

>1xh1A (length=496) Species: 9606 (Homo sapiens)

QYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVA
IYNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVIN
HMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIEN
YNDATQVRDCRLTGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASK
HMWPGDIKAILDKLHNLNSNWFPAGSKPFIYQEVIDLGGEPIKSSDYFGN
GRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFVPSDRALVFVDSHD
NQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRQFQN
GNDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVIFRNV
VDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWSFSLTLQTGLPAGTYC
DVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL

3D structure

• PDB: 1xh1 Structural and mechanistic studies of chloride induced activation of human pancreatic alpha-amylase
• Chain: A
• Resolution: 2.03 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D197
• Catalytic site (residue number reindexed from 1): D197
• 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)	Binding affinity
BS01	CA	A	N100 R158 D167 H201	N100 R158 D167 H201
BS02	CL	A	R195 R337	R195 R337

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
• GO:0044245 polysaccharide digestion

Cellular Component

• GO:0005576 extracellular region
• GO:0005615 extracellular space
• GO:0070062 extracellular exosome

External links

• PDB: RCSB:1xh1, PDBe:1xh1, PDBj:1xh1
• PDBsum: 1xh1
• PubMed: 15722449
• UniProt: P04746|AMYP_HUMAN Pancreatic alpha-amylase (Gene Name=AMY2A)