Structure of PDB 3vx0 Chain A

Receptor sequence
>3vx0A (length=475) Species: 510516 (Aspergillus oryzae RIB40) [Search protein sequence]
ATPADWRSQSIYFLLTDRFARTDGSTTATCNTADQKYCGGTWQGIIDKLD
YIQGMGFTAIWITPVTAQLPQTTAYGDAYHGYWQQDIYSLNENYGTADDL
KALSSALHERGMYLMVDVVANHMGYDGAGSSVDYSVFKPFSSQDYFHPFC
FIQNYEDQTQVEDCWLGDNTVSLPDLDTTKDVVKNEWYDWVGSLVSNYSI
DGLRIDTVKHVQKDFWPGYNKAAGVYCIGEVLDGDPAYTCPYQNVMDGVL
NYPIYYPLLNAFKSTSGSMDDLYNMINTVKSDCPDSTLLGTFVENHDNPR
FASYTNDIALAKNVAAFIILNDGIPIIYAGQEQHYAGGNDPANREATWLS
GYPTDSELYKLIASANAIRNYAISKDTGFVTYKNWPIYKDDTTIAMRKGT
DGSQIVTILSNKGASGDSYTLSLSGAGYTAGQQLTEVIGCTTVTVGSDGN
VPVPMAGGLPRVLYPTEKLAGSKIC
3D structure
PDB3vx0 Crystal Structure of alpha-amylase from Aspergillus oryzae
ChainA
Resolution1.5 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 CA A N121 E162 D175 H210 N121 E162 D175 H210
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0005509 calcium ion binding
GO:0016798 hydrolase activity, acting on glycosyl bonds
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:0009277 fungal-type cell wall
GO:0030287 cell wall-bounded periplasmic space
GO:0030428 cell septum
GO:0031521 spitzenkorper
GO:0032163 hyphal septin band

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3vx0, PDBe:3vx0, PDBj:3vx0
PDBsum3vx0
PubMed
UniProtP0C1B3|AMYA1_ASPOR Alpha-amylase A type-1/2 (Gene Name=amy1)

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