Structure of PDB 1wds Chain A

Receptor sequence

>1wdsA (length=492) Species: 3847 (Glycine max)

DSNMLLNYVPVYVMLPLGVVNVDNVFEDPDGLKEQLLQLRAAGVDGVMVD
VWWGIIELKGPKQYDWRAYRSLLQLVQECGLTLQAIMSFHQCGGNVGDIV
NIPIPQWVLDIGESNHDIFYTNRSGTRNKEYLTVGVDNEPIFHGRTAIEI
YSDYMKSFRENMSDFLESGLIIDIEVGLGPAGELRYPSYPQSQGWEFPGI
GEFQCYDKYLKADFKAAVARAGHPEWELPDDAGKYNDVPESTGFFKSNGT
YVTEKGKFFLTWYSNKLLNHGDQILDEANKAFLGCKVKLAIKVSGIHWWY
KVENHAAELTAGYYNLNDRDGYRPIARMLSRHHAILNFACLEMRDSEQPS
DAKSGPQELVQQVLSGGWREDIRVAGENALPRYDATAYNQIILNARPQGV
NNNGPPKLSMFGVTYLRLSDDLLQKSNFNIFKKFVLKMHADQDYCANPQK
YNHAITPLKPSAPKIPIEVLLEATKPTLPFPWLPETDMKVDG

3D structure

• PDB: 1wds Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism.
• Chain: A
• Resolution: 1.64 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D101 E186 A342 E380 L383
• Catalytic site (residue number reindexed from 1): D98 E183 A339 E377 L380
• 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	E186 K295 E380 A382	E183 K292 E377 A379
BS02	GLC	A	D53 H93 D101 R420	D50 H90 D98 R417
BS03	GLC	A	V99 W198 F200 H300 W301 M346	V96 W195 F197 H297 W298 M343

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:1wds, PDBe:1wds, PDBj:1wds
• PDBsum: 1wds
• PubMed: 15794648
• UniProt: P10538|AMYB_SOYBN Beta-amylase (Gene Name=BMY1)