Structure of PDB 3olg Chain A

Receptor sequence
>3olgA (length=495) Species: 9606 (Homo sapiens) [Search protein sequence]
YSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAI
YNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINH
MCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENY
NDATQVRDCRLTGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKH
MWPGDIKAILDKLHNLNSNWFPAGSKPFIYQEVIDLGGEPIKSSDYFGNG
RVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDN
QRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRQFQNG
NDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVIFRNVV
DGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWSFSLTLQTGLPAGTYCD
VISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL
3D structure
PDB3olg Structures of human pancreatic alpha-amylase in complex with acarviostatins: Implications for drug design against type II diabetes.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D197 S226 D300
Catalytic site (residue number reindexed from 1) D196 S225 D299
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 GLC A W58 W59 Q63 H305 W57 W58 Q62 H304 PDBbind-CN: -logKd/Ki=7.84,Ki=14.3nM
BS02 G6D A W59 T163 W58 T162 PDBbind-CN: -logKd/Ki=7.84,Ki=14.3nM
BS03 GLC A Y151 K200 E240 G306 Y150 K199 E239 G305 PDBbind-CN: -logKd/Ki=7.84,Ki=14.3nM
BS04 G6D A H201 E233 D300 G306 H200 E232 D299 G305 PDBbind-CN: -logKd/Ki=7.84,Ki=14.3nM
BS05 GLC A W134 K172 Y174 W133 K171 Y173 PDBbind-CN: -logKd/Ki=7.84,Ki=14.3nM
BS06 GLC A S132 W134 D135 Y174 S131 W133 D134 Y173 PDBbind-CN: -logKd/Ki=7.84,Ki=14.3nM
BS07 BGC A K140 E171 W203 D206 K139 E170 W202 D205 PDBbind-CN: -logKd/Ki=7.84,Ki=14.3nM
BS08 CA A N100 R158 D167 H201 N99 R157 D166 H200
BS09 HSD A W58 Y62 H101 D197 E233 H299 D300 W57 Y61 H100 D196 E232 H298 D299 PDBbind-CN: -logKd/Ki=7.84,Ki=14.3nM
BS10 PCA A Y2 P228 F229 I230 N250 Y1 P227 F228 I229 N249
BS11 GLC A K322 T377 W388 Q390 K321 T376 W387 Q389 PDBbind-CN: -logKd/Ki=7.84,Ki=14.3nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3olg, PDBe:3olg, PDBj:3olg
PDBsum3olg
PubMed21111049
UniProtP04746|AMYP_HUMAN Pancreatic alpha-amylase (Gene Name=AMY2A)

[Back to BioLiP]