Structure of PDB 4iib Chain A

Receptor sequence
>4iibA (length=834) Species: 5053 (Aspergillus aculeatus) [Search protein sequence]
LAFSPPFYPSPWANGQGEWAEAYQRAVAIVSQMTLDEKVNLTTGTGWELE
KCVGQTGGVPRLNIGGMCLQDSPLGIRDSDYNSAFPAGVNVAATWDKNLA
YLRGQAMGQEFSDKGIDVQLGPAAGPLGRSPDGGRNWEGFSPDPALTGVL
FAETIKGIQDAGVVATAKHYILNEQEHFRQVAEAAGYGFNISDTISSNVD
DKTIHEMYLWPFADAVRAGVGAIMCSYNQINNSYGCQNSYTLNKLLKAEL
GFQGFVMSDWGAHHSGVGSALAGLDMSMPGDITFDSATSFWGTNLTIAVL
NGTVPQWRVDDMAVRIMAAYYKVGRDRLYQPPNFSSWTRDEYGFKYFYPQ
EGPYEKVNHFVNVQRNHSEVIRKLGADSTVLLKNNNALPLTGKERKVAIL
GEDAGSNSYGANGCSDRGCDNGTLAMAWGSGTAEFPYLVTPEQAIQAEVL
KHKGSVYAITDNWALSQVETLAKQASVSLVFVNSDAGEGYISVDGNEGDR
NNLTLWKNGDNLIKAAANNCNNTIVVIHSVGPVLVDEWYDHPNVTAILWA
GLPGQESGNSLADVLYGRVNPGAKSPFTWGKTREAYGDYLVRELNNGNGA
PQDDFSEGVFIDYRGFDKRNETPIYEFGHGLSYTTFNYSGLHIQVLNAVA
TETGAAPTFGQVGNASDYVYPEGLTRISKFIYPWLNSTDLKASSGDPYYG
VDTAEHVPEGATDGSPQPVLPAGGGSGGNPRLYDELIRVSVTVKNTGRVA
GDAVPQLYVSLGGPNEPKVVLRKFDRLTLKPSEETVWTTTLTRRDLSNWD
VAAQDWVITSYPKKVHVGSSSRQLPLHAALPKVQ
3D structure
PDB4iib Crystal structures of glycoside hydrolase family 3 beta-glucosidase 1 from Aspergillus aculeatus
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) D280 A507
Catalytic site (residue number reindexed from 1) D259 A486
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 Y724 H732 Y698 H706
BS02 MAN A Q258 H285 S286 Q237 H264 S265
BS03 MAN A D214 H285 D193 H264
BS04 MAN A Q258 H732 Q237 H706
BS05 MAN A S25 P27 S4 P6
BS06 MAN A D728 H732 D702 H706
BS07 MAN A W484 A485 Q488 W463 A464 Q467
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
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009251 glucan catabolic process
GO:0030245 cellulose catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4iib, PDBe:4iib, PDBj:4iib
PDBsum4iib
PubMed23537284
UniProtP48825|BGL1_ASPAC Beta-glucosidase 1

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