Structure of PDB 6yqc Chain BBB

Receptor sequence
>6yqcBBB (length=476) Species: 5062 (Aspergillus oryzae) [Search protein sequence]
ATPADWRSQSIYFLLTDRFARTDGSTTATCNTADQKYCGGTWQGIIDKLD
YIQGMGFTAIWITPVTAQLPQTTAYGDAYHGYWQQDIYSLNENYGTADDL
KALSSALHERGMYLMVDVVANHMGYDGAGSSVDYSVFKPFSSQDYFHPFC
FIQNYEDQTQVEDCWLGDNTVSLPDLDTTKDVVKNEWYDWVGSLVSNYSI
DGLRIDTVKHVQKDFWPGYNKAAGVYCIGEVLDGDPAYTCPYQNVMDGVL
NYPIYYPLLNAFKSTSGSMDDLYNMINTVKSDCPDSTLLGTFVENHDNPR
FASYTNDIALAKNVAAFIILNDGIPIIYAGQEQHYAGGNDPANREATWLS
GYPTDSELYKLIASANAIRNYAISKDTGFVTYKNWPIYKDDTTIAMRKGT
DGSQIVTILSNKGASGDSYTLSLSGAGYTAGQQLTEVIGCTTVTVGSDGN
VPVPMAGGLPRVLYPTEKLAGSKICS
3D structure
PDB6yqc Activity-Based Protein Profiling of Retaining alpha-Amylases in Complex Biological Samples.
ChainBBB
Resolution1.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R204 D206 E230 H296 D297
Catalytic site (residue number reindexed from 1) R204 D206 E230 H296 D297
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 QJN BBB Y75 H80 Y82 W83 H122 R204 D206 T207 H296 D297 D340 R344 Y75 H80 Y82 W83 H122 R204 D206 T207 H296 D297 D340 R344
BS02 CA BBB N121 E162 D175 H210 N121 E162 D175 H210
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0005509 calcium ion binding
GO:0043169 cation binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0016052 carbohydrate catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6yqc, PDBe:6yqc, PDBj:6yqc
PDBsum6yqc
PubMed33497208
UniProtA0A1S9DH83

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