Structure of PDB 1q6f Chain A

Receptor sequence
>1q6fA (length=490) Species: 3847 (Glycine max) [Search protein sequence]
NMLLNYVPVYVMLPLGVVNVDNVFEDPDGLKEQLLQLRAAGVDGVMVDVW
WGIIELKGPKQYDWRAYRSLLQLVQECGLTLQAIMSFHQCGGNVGDIVNI
PIPQWVLDIGESNHDIFYTNRSGTRNKEYLTVGVDNEPIFHGRTAIEIYS
DYMKSFRENMSDFLESGLIIDIYVGLGPAGELRYPSYPQSQGWEFPGIGE
FQCYDKYLKADFKAAVARAGHPEWELPDDAGKYNDVPESTGFFKSNGTYV
TEKGKFFLTWYSNKLLNHGDQILDEANKAFLGCKVKLAIKVSGIHWWYKV
ENHAAELTAGYYNLNDRDGYRPIARMLSRHHAILNFTCLEMRDSEQPSDA
KSGPQELVQQVLSGGWREDIRVAGENALPRYDATAYNQIILNARPQGVNN
NGPPKLSMFGVTYLRLSDDLLQKSNFNIFKKFVLKMHADQDYCANPQKYN
HAITPLKPSAPKIPIEVLLEATKPTLPFPWLPETDMKVDG
3D structure
PDB1q6f Structural and Enzymatic Analysis of Soybean {beta}-Amylase Mutants with Increased pH Optimum
ChainA
Resolution2.1 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 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 BGC A K295 T342 E380 A382 K290 T337 E375 A377
BS02 BGC A D53 H93 D101 R420 D48 H88 D96 R415
BS03 BGC A V99 H300 M346 V94 H295 M341
BS04 GLC A E186 R188 Y192 G298 T342 E181 R183 Y187 G293 T337
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:1q6f, PDBe:1q6f, PDBj:1q6f
PDBsum1q6f
PubMed14638688
UniProtP10538|AMYB_SOYBN Beta-amylase (Gene Name=BMY1)

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