Structure of PDB 1byc Chain A

Receptor sequence

>1bycA (length=490) Species: 3847 (Glycine max)

SNMLLNYVPVYVMLPLGVVNVDNVFEDPDGLKEQLLQLRAAGVDGVMVDV
WWGIIELKGPKQYDWRAYRSLFQLVQECGLTLQAIMSFHQCGGNVGDIVN
IPIPQWVLDIGESNHDIFYTNRSGTRNKEYLTVGVDNEPIFHGRTAIEIY
SDYMKSFRENMSDFLESGLIIDIEVGLGPAGELRYPSYPQSQGWEFPRIG
EFQCYDKYLKADFKAAVARAGHPEWELPDDAGKYNDVPESTGFFKSNGTY
VTEKGKFFLTWYSNKLLNHGDQILDEANKAFLGCKVKLAIKVSGIHWWYK
VENHAAELTAGYYNLNDRDGYRPIARMLSRHHAILNFTCLEMRDSEQPSD
AKSGPQELVQQVLSGGWREDIRVAGENALPRYDATAYNQIILNAKPQGVN
NNGPPKLSMFGVTYLRLSDDLLQKSNFNIFKKFVLKMHADQDYCANPQKY
NHAITPLKPSAPKIPIEVLLEATKPTLPFPWLPETDMKVD

3D structure

• PDB: 1byc Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D101 E186 T342 E380 L383
• Catalytic site (residue number reindexed from 1): D97 E182 T338 E376 L379
• 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	BGC	A	H300 M346 D494	H296 M342 D490
BS02	GLC	A	E186 R188 Y192 S297 G298 T342	E182 R184 Y188 S293 G294 T338
BS03	GLC	A	E186 K295 T342 E380 A382	E182 K291 T338 E376 A378
BS04	GLC	A	D53 H93 D101 R420	D49 H89 D97 R416

Gene Ontology

Molecular Function

• GO:0016161 beta-amylase activity
• GO:0016798 hydrolase activity, acting on glycosyl bonds

Biological Process

• GO:0000272 polysaccharide catabolic process

External links

• PDB: RCSB:1byc, PDBe:1byc, PDBj:1byc
• PDBsum: 1byc
• PubMed: 8011643
• UniProt: P10538|AMYB_SOYBN Beta-amylase (Gene Name=BMY1)