Structure of PDB 4iic Chain B

Receptor sequence
>4iicB (length=832) Species: 5053 (Aspergillus aculeatus) [Search protein sequence]
LAFSPPFYPSPWANGQGEWAEAYQRAVAIVSQMTLDEKVNLTTGTGWELE
KCVGQTGGVPRLNIGGMCLQDSPLGIRDSDYNSAFPAGVNVAATWDKNLA
YLRGQAMGQEFSDKGIDVQLGPAAGPLGRSPDGGRNWEGFSPDPALTGVL
FAETIKGIQDAGVVATAKHYILNEQEHFRQVAEAAGYGFNISDTISSNVD
DKTIHEMYLWPFADAVRAGVGAIMCSYNQINNSYGCQNSYTLNKLLKAEL
GFQGFVMSDWGAHHSGVGSALAGLDMSMPGDITFDSATSFWGTNLTIAVL
NGTVPQWRVDDMAVRIMAAYYKVGRDRLYQPPNFSSWTRDEYGFKYFYPQ
EGPYEKVNHFVNVQRNHSEVIRKLGADSTVLLKNNNALPLTGKERKVAIL
GEDAGSNSYGANGCSDRGCDNGTLAMAWGSGTAEFPYLVTPEQAIQAEVL
KHKGSVYAITDNWALSQVETLAKQASVSLVFVNSDAGEGYISVDGNEGDR
NNLTLWKNGDNLIKAAANNCNNTIVVIHSVGPVLVDEWYDHPNVTAILWA
GLPGQESGNSLADVLYGRVNPGAKSPFTWGKTREAYGDYLVRELNNGNGA
PQDDFSEGVFIDYRGFDKRNETPIYEFGHGLSYTTFNYSGLHIQVLNATE
TGAAPTFGQVGNASDYVYPEGLTRISKFIYPWLNSTDLKASSGDPYYGVD
TAEHVPEGATDGSPQPVLPAGGGSGGNPRLYDELIRVSVTVKNTGRVAGD
AVPQLYVSLGGPNEPKVVLRKFDRLTLKPSEETVWTTTLTRRDLSNWDVA
AQDWVITSYPKKVHVGSSSRQLPLHAALPKVQ
3D structure
PDB4iic Crystal structures of glycoside hydrolase family 3 beta-glucosidase 1 from Aspergillus aculeatus
ChainB
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) 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 B Y724 H732 Y696 H704
BS02 MAN B Q258 H285 S286 Q237 H264 S265
BS03 MAN B Q258 H732 P734 Q237 H704 P706
BS04 MAN B S25 P27 S4 P6
BS05 MAN B D728 H732 D700 H704
BS06 MAN B W484 A485 Q488 W463 A464 Q467
BS07 IFM B V74 D92 R156 K189 H190 M245 Y248 D280 W281 S451 E509 V53 D71 R135 K168 H169 M224 Y227 D259 W260 S430 E488 MOAD: Ki=14uM
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
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Biological Process
External links
PDB RCSB:4iic, PDBe:4iic, PDBj:4iic
PDBsum4iic
PubMed23537284
UniProtP48825|BGL1_ASPAC Beta-glucosidase 1

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