Structure of PDB 1bfn Chain A

Receptor sequence
>1bfnA (length=490) Species: 3847 (Glycine max) [Search protein sequence]
NMLLNYVPVYVMLPLGVVNVDNVFEDPDGLKEQLLQLRAAGVDGVMVDVW
WGIIELKGPKQYDWRAYRSLLQLVQECGLTLQAIMSFHQCGGNVGDIVNI
PIPQWVLDIGESNHDIFYTNRSGTRNKEYLTVGVDNEPIFHGRTAIEIYS
DYMKSFRENMSDFLESGLIIDIEVGLGPAGELRYPSYPQSQGWEFPGIGE
FQCYDKYLKADFKAAVARAGHPEWELPDDAGKYNDVPESTGFFKSNGTYV
TEKGKFFLTWYSNKLLNHGDQILDEANKAFLGCKVKLAIKVSGIHWWYKV
ENHAAELTAGYYNLNDRDGYRPIARMLSRHHAILNFTCLEMRDSEQPSDA
KSGPQELVQQVLSGGWREDIRVAGENALPRYDATAYNQIILNARPQGVNN
NGPPKLSMFGVTYLRLSDDLLQKSNFNIFKKFVLKMHADQDYCANPQKYN
HAITPLKPSAPKIPIEVLLEATKPTLPFPWLPETDMKVDG
3D structure
PDB1bfn Crystal structure of recombinant soybean beta-amylase complexed with beta-cyclodextrin.
ChainA
Resolution2.07 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) D101 E186 T342 E380 L383
Catalytic site (residue number reindexed from 1) D96 E181 T337 E375 L378
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 GLC A F200 L383 F195 L378
BS02 GLC A W198 F200 H300 M346 W193 F195 H295 M341
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:1bfn, PDBe:1bfn, PDBj:1bfn
PDBsum1bfn
PubMed9677422
UniProtP10538|AMYB_SOYBN Beta-amylase (Gene Name=BMY1)

[Back to BioLiP]