Structure of PDB 1kxq Chain C

Receptor sequence

>1kxqC (length=496) Species: 9823 (Sus scrofa)

QYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIV
VTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVIN
HMCGSGAAAGTGTTCGSYCNPGSREFPAVPYSAWDFNDGKCKTASGGIES
YNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASK
HMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAIKSSEYFGN
GRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHD
NQRGHGAGGSSILTFWDARLYKIAVGFMLAHPYGFTRVMSSYRWARNFVN
GEDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWREIRNMVWFRNV
VDGQPFANWWDNGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYC
DVISGDKVGNSCTGIKVYVSSDGTAQFSISNSAEDPFIAIHAESKL

3D structure

• PDB: 1kxq Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology.
• Chain: C
• Resolution: 1.6 Å

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)	Binding affinity
BS01	CA	C	N100 R158 D167 H201	N100 R158 D167 H201

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

External links

• PDB: RCSB:1kxq, PDBe:1kxq, PDBj:1kxq
• PDBsum: 1kxq
• PubMed: 11960990
• UniProt: P00690|AMYP_PIG Pancreatic alpha-amylase (Gene Name=AMY2)