Structure of PDB 1fa2 Chain A

Receptor sequence
>1fa2A (length=498) Species: 4120 (Ipomoea batatas) [Search protein sequence]
APIPGVMPIGNYVSLYVMLPLGVVNADNVFPDKEKVEDELKQVKAGGCDG
VMVDVWWGIIEAKGPKQYDWSAYRELFQLVKKCGLKIQAIMSFHQCGGNV
GDAVFIPIPQWILQIGDKNPDIFYTNRAGNRNQEYLSLGVDNQRLFQGRT
ALEMYRDFMESFRDNMADFLKAGDIVDIEVGCGAAGELRYPSYPETQGWV
FPGIGEFQCYDKYMVADWKEAVKQAGNADWEMPGKGAGTYNDTPDKTEFF
RPNGTYKTDMGKFFLTWYSNKLIIHGDQVLEEANKVFVGLRVNIAAKVSG
IHWWYNHVSHAAELTAGFYNVAGRDGYRPIARMLARHHATLNFTCLEMRD
SEQPAEAKSAPQELVQQVLSSGWKEYIDVAGENALPRYDATAYNQMLLKL
RPNGVNLNGPPKLKMSGLTYLRLSDDLLQTDNFELFKKFVKKMHADLDPS
PNAISPAVLERSNSAITIDELMEATKGSRPFPWYDVTDMPVDGSNPFD
3D structure
PDB1fa2 Crystallization, molecular replacement solution, and refinement of tetrameric beta-amylase from sweet potato.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D102 E187 T344 E382 L385
Catalytic site (residue number reindexed from 1) D102 E187 T344 E382 L385
Enzyme Commision number 3.2.1.2: beta-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 RR7 A E187 Y193 G300 C345 E187 Y193 G300 C345
BS02 GLC A H302 M348 H302 M348
Gene Ontology
Molecular Function
GO:0016161 beta-amylase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0000272 polysaccharide catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1fa2, PDBe:1fa2, PDBj:1fa2
PDBsum1fa2
PubMed7777485
UniProtP10537|AMYB_IPOBA Beta-amylase (Gene Name=BMY1)

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