Structure of PDB 5ju6 Chain A

Receptor sequence
>5ju6A (length=835) Species: 68825 (Rasamsonia emersonii) [Search protein sequence]
NLAYSPPFYPSPWANGQGDWAEAYQKAVQFVSQLTLAEKVNLTTGTGWEQ
DRCVGQVGSIPRLGFPGLCMQDSPLGVRDTDYNSAFPAGVNVAATWDRNL
AYRRGVAMGEEHRGKGVDVQLGPVAGPLGRSPDAGRNWEGFAPDPVLTGN
MMASTIQGIQDAGVIACAKHFILYEQEHFRQGAQDGYDISDSISANADDK
TMHELYLWPFADAVRAGVGSVMCSYNQVNNSYACSNSYTMNKLLKSELGF
QGFVMTDWGGHHSGVGSALAGLDMSMPGDIAFDSGTSFWGTNLTVAVLNG
SIPEWRVDDMAVRIMSAYYKVGRDRYSVPINFDSWTLDTYGPEHYAVGQG
QTKINEHVDVRGNHAEIIHEIGAASAVLLKNKGGLPLTGTERFVGVFGKD
AGSNPWGVNGCSDRGCDNGTLAMGWGSGTANFPYLVTPEQAIQREVLSRN
GTFTGITDNGALAEMAAAASQADTCLVFANADSGEGYITVDGNEGDRKNL
TLWQGADQVIHNVSANCNNTVVVLHTVGPVLIDDWYDHPNVTAILWAGLP
GQESGNSLVDVLYGRVNPGKTPFTWGRARDDYGAPLIVKPNNGKGAPQQD
FTEGIFIDYRRFDKYNITPIYEFGFGLSYTTFEFSQLNVQPINAPPYTPA
SGFTKAAQSFGQPSNASDNLYPSDIERVPLYIYPWLNSTDLKASANDPDY
GLPTEKYVPPNATNGDPQPIDPAGGAPGGNPSLYEPVARVTTIITNTGKV
TGDEVPQLYVSLGGPDDAPKVLRGFDRITLAPGQQYLWTTTLTRRDISNW
DPVTQNWVVTNYTKTIYVGNSSRNLPLQAPLKPYP
3D structure
PDB5ju6 Structural and functional studies of the glycoside hydrolase family 3 beta-glucosidase Cel3A from the moderately thermophilic fungus Rasamsonia emersonii.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D277 S503
Catalytic site (residue number reindexed from 1) D257 S483
Enzyme Commision number 3.2.1.21: beta-glucosidase.
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 BMA A P822 V823 P802 V803
BS02 MAN A S255 Y727 P729 S235 Y707 P709
BS03 MAN A Y24 S25 P27 Y4 S5 P7
BS04 BGC A V74 D92 R156 K189 H190 Y245 D277 W278 S447 E505 V54 D72 R136 K169 H170 Y225 D257 W258 S427 E485
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5ju6, PDBe:5ju6, PDBj:5ju6
PDBsum5ju6
PubMed27377383
UniProtQ8TGI8

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