Structure of PDB 3wq5 Chain A

Receptor sequence
>3wq5A (length=475) Species: 4442 (Camellia sinensis) [Search protein sequence]
SFNRTSFPDGFVFGAASSAYQFEGAAKEGGKGPNIWDTFTHEFPGKISNG
STGDVADDFYHRYKEDVKVLKFIGLDGFRMSISWARVLPRGKLSGGVNKE
GIAFYNNVINDLLSKGIQPFITIFHWDLPQALEDEYGGFLSPHIVNDFRD
FAELCFKEFGDRVKHWITMNEPWSYSYGGYDAGLLAPGRCSAFMAFCPKG
NSGTEPYIVTHNLLLSHAAAVKLYKEKYQAYQKGQIGITLVTYWMIPYSN
SKADKDAAQRALDFMYGWFIEPLSFGEYPKSMRRLVGKRLPRFTKEQAML
VKGSFDFLGLNYYIANYVLNVPTSNSVNLSYTTDSLSNQTAFRNGVAIGR
PTGVPAFFMYPKGLKDLLVYTKEKYNDPVIYITENGMGDNNNVTTEEGIK
DPQRVYFYNQHLLSLKNAIAAGVKVKGYFTWAFLDNFEWLSGYTQRFGIV
YVDFKDGLKRYPKHSALWFKKFLLK
3D structure
PDB3wq5 Crystal structures of beta-primeverosidase in complex with disaccharide amidine inhibitors.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R111 H157 E203 S206 N343 Y345 E416
Catalytic site (residue number reindexed from 1) R79 H125 E171 S174 N311 Y313 E384
Enzyme Commision number 3.2.1.149: beta-primeverosidase.
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 VPA A Q53 H157 N202 E203 S206 Y345 F389 E416 W463 E470 W471 S473 Q477 F479 Q21 H125 N170 E171 S174 Y313 F357 E384 W431 E438 W439 S441 Q445 F447 PDBbind-CN: -logKd/Ki=3.85,Ki=140uM
BS02 VPA A A58 K59 K63 G64 P65 P121 R122 A163 A26 K27 K31 G32 P33 P89 R90 A131 PDBbind-CN: -logKd/Ki=3.85,Ki=140uM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0050535 beta-primeverosidase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3wq5, PDBe:3wq5, PDBj:3wq5
PDBsum3wq5
PubMed24753293
UniProtQ7X9A9

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