Structure of PDB 3zyz Chain A

Receptor sequence
>3zyzA (length=713) Species: 51453 (Trichoderma reesei) [Search protein sequence]
VVPPAGTPWGTAYDKAKAALAKLNLQDKVGIVSGVGWNGGPCVGNTSPAS
KISYPSLCLQDGPLGVRYSTGSTAFTPGVQAASTWDVNLIRERGQFIGEE
VKASGIHVILGPVAGPLGKTPQGGRNWEGFGVDPYLTGIAMGQTINGIQS
VGVQATAKHYILNEQELNRETISSNPDDRTLHELYTWPFADAVQANVASV
MCSYNKVNTTWACEDQYTLQTVLKDQLGFPGYVMTDWNAQHTTVQSANSG
LDMSMPGTDFNGNNRLWGPALTNAVNSNQVPTSRVDDMVTRILAAWYLTG
QDQAGYPSFNISRNVQGNHKTNVRAIARDGIVLLKNDANILPLKKPASIA
VVGSAAIIGNHARNSPSCNDKGCDDGALGMGWGSGAVNYPYFVAPYDAIN
TRASSQGTQVTLSNTDNTSSGASAARGKDVAIVFITADSGEGYITVEGNA
GDRNNLDPWHNGNALVQAVAGANSNVIVVVHSVGAIILEQILALPQVKAV
VWAGLPSQESGNALVDVLWGDVSPSGKLVYTIAKSPNDYNTRIVSGGSDS
FSEGLFIDYKHFDDANITPRYEFGYGLSYTKFNYSRLSVLSTAKSGPATG
AVVPGGPSDLFQNVATVTVDIANSGQVTGAEVAQLYITYPSSAPRTPPKQ
LRGFAKLNLTPGQSGTATFNIRRRDLSYWDTASQKWVVPSGSFGISVGAS
SRDIRLTSTLSVA
3D structure
PDB3zyz Biochemical Characterization and Crystal Structures of a Fungal Family 3 Beta-Glucosidase, Cel3A from Hypocrea Jecorina.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D236 S439
Catalytic site (residue number reindexed from 1) D236 S439
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 BGC A D61 R125 K158 H159 Y204 D236 W237 S384 E441 D61 R125 K158 H159 Y204 D236 W237 S384 E441
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:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process
GO:0009251 glucan catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3zyz, PDBe:3zyz, PDBj:3zyz
PDBsum3zyz
PubMed25164811
UniProtQ12715

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