Structure of PDB 4iih Chain A

Receptor sequence
>4iihA (length=833) Species: 5053 (Aspergillus aculeatus) [Search protein sequence]
LAFSPPFYPSPWANGQGEWAEAYQRAVAIVSQMTLDEKVNLTTGTGWELE
KCVGQTGGVPRLNIGGMCLQDSPLGIRDSDYNSAFPAGVNVAATWDKNLA
YLRGQAMGQEFSDKGIDVQLGPAAGPLGRSPDGGRNWEGFSPDPALTGVL
FAETIKGIQDAGVVATAKHYILNEQEHFRQVAEAAGYGFNISDTISSNVD
DKTIHEMYLWPFADAVRAGVGAIMCSYNQINNSYGCQNSYTLNKLLKAEL
GFQGFVMSDWGAHHSGVGSALAGLDMSMPGDITFDSATSFWGTNLTIAVL
NGTVPQWRVDDMAVRIMAAYYKVGRDRLYQPPNFSSWTRDEYGFKYFYPQ
EGPYEKVNHFVNVQRNHSEVIRKLGADSTVLLKNNNALPLTGKERKVAIL
GEDAGSNSYGANGCSDRGCDNGTLAMAWGSGTAEFPYLVTPEQAIQAEVL
KHKGSVYAITDNWALSQVETLAKQASVSLVFVNSDAGEGYISVDGNEGDR
NNLTLWKNGDNLIKAAANNCNNTIVVIHSVGPVLVDEWYDHPNVTAILWA
GLPGQESGNSLADVLYGRVNPGAKSPFTWGKTREAYGDYLVRELNNGNGA
PQDDFSEGVFIDYRGFDKRNETPIYEFGHGLSYTTFNYSGLHIQVLNVAT
ETGAAPTFGQVGNASDYVYPEGLTRISKFIYPWLNSTDLKASSGDPYYGV
DTAEHVPEGATDGSPQPVLPAGGGSGGNPRLYDELIRVSVTVKNTGRVAG
DAVPQLYVSLGGPNEPKVVLRKFDRLTLKPSEETVWTTTLTRRDLSNWDV
AAQDWVITSYPKKVHVGSSSRQLPLHAALPKVQ
3D structure
PDB4iih Crystal structures of glycoside hydrolase family 3 beta-glucosidase 1 from Aspergillus aculeatus
ChainA
Resolution2.0 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 Y697 H705
BS02 MAN A Q258 H285 S286 Q237 H264 S265
BS03 MAN A Q258 H732 Q237 H705
BS04 MAN A S25 P27 S4 P6
BS05 MAN A D728 H732 D701 H705
BS06 MAN A W484 A485 Q488 W463 A464 Q467
BS07 MAN A T359 D361 T338 D340
BS08 SGC A R98 Y511 R77 Y490
BS09 BGC A V74 D92 R98 D280 W281 S451 E509 V53 D71 R77 D259 W260 S430 E488
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:4iih, PDBe:4iih, PDBj:4iih
PDBsum4iih
PubMed23537284
UniProtP48825|BGL1_ASPAC Beta-glucosidase 1

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