Structure of PDB 1bvn Chain P

Receptor sequence
>1bvnP (length=496) Species: 9823 (Sus scrofa) [Search protein sequence]
QYAPQTQSGRTDIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENVV
VTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVIN
HMCGSGAAAGTGTTCGSYCNPGSREFPAVPYSAWDFNDGKCKTASGGIES
YNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRLDASK
HMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAISSSEYFGN
GRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHD
NQRGHGAGGSSILTFWDARLYKVAVGFMLAHPYGFTRVMSSYRWARNFVN
GEDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWREIRNMVWFRNV
VDGQPFANWWDNGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYC
NVISGDKVGNSCTGIKVYVSSDGTAQFSISNSAQDPFIAIHAESKL
3D structure
PDB1bvn The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat.
ChainP
Resolution2.5 Å
3D
structure
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Enzymatic activity
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 P 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1bvn, PDBe:1bvn, PDBj:1bvn
PDBsum1bvn
PubMed7897663
UniProtP00690|AMYP_PIG Pancreatic alpha-amylase (Gene Name=AMY2)

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