Structure of PDB 1v3i Chain A

Receptor sequence
>1v3iA (length=490) Species: 3847 (Glycine max) [Search protein sequence]
NMLLNYVPVYVMLPLGVVNVDNVFEDPDGLKEQLLQLRAAGVDGVMVDVW
WGIIELKGPKQYDWRAYRSLLQLVQECGLTLQAIMSFHQCGGNVGDIVNI
PIPQWVLDIGESNHDIFYTNRSGTRNKEYLTVGVDNEPIFHGRTAIEIYS
DYMKSFRENMSDFLESGLIIDIEVGLGPAGELRYPSYPQSQGWEFPGIGE
FQCYDKYLKADFKAAVARAGHPEWELPDDAGKYNDVPESTGFFKSNGTYV
TEKGKFFLTWYSNKLLNHGDQILDEANKAFLGCKVKLAIKVSGIHWWYKV
ENHAAELTAGYYNLNDRDGYRPIARMLSRHHAILNFTCLEMRDSEQPSDA
KSGPQELVQQVLSGGWREDIRVAGQNALPRYDATAYNQIILNARPQGVNN
NGPPKLSMFGVTYLRLSDDLLQKSNFNIFKKFVLKMHADQDYCANPQKYN
HAITPLKPSAPKIPIEVLLEATKPTLPFPWLPETDMKVDG
3D structure
PDB1v3i The Roles of Glu186 and Glu380 in the Catalytic Reaction of Soybean beta-Amylase.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D101 E186 T342 Q380 L383
Catalytic site (residue number reindexed from 1) D96 E181 T337 Q375 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 E186 K295 T342 Q380 A382 E181 K290 T337 Q375 A377
BS02 GLC A D53 H93 D101 R420 D48 H88 D96 R415
BS03 GLC A W198 F200 H300 W301 W193 F195 H295 W296
Gene Ontology
Molecular Function
GO:0016161 beta-amylase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0000272 polysaccharide catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1v3i, PDBe:1v3i, PDBj:1v3i
PDBsum1v3i
PubMed15178253
UniProtP10538|AMYB_SOYBN Beta-amylase (Gene Name=BMY1)

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