Structure of PDB 5gm4 Chain E

Receptor sequence
>5gm4E (length=219) Species: 5053 (Aspergillus aculeatus) [Search protein sequence]
AQLCDQYATYTGGVYTINNNLWGKDAGSGSQCTTVNSASSAGTSWSTKWN
WSGGENSVKSYANSGLTFNKKLVSQISQIPTTARWSYDNTGIRADVAYDL
FTAADINHVTWSGDYELMIWLARYGGVQPIGSQIATATVDGQTWELWYGA
NGSQKTYSFVAPTPITSFQGDVNDFFKYLTQNHGFPASSQYLITLQFGTA
PFTGGPATLSVSNWSASVQ
3D structure
PDB5gm4 Crystal structure and genetic modifications of FI-CMCase from Aspergillus aculeatus F-50
ChainE
Resolution1.92 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E118 A202
Catalytic site (residue number reindexed from 1) E116 A200
Enzyme Commision number 3.2.1.4: cellulase.
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 E D97 I132 D95 I130
BS02 BGC E W24 Y63 E118 M120 Q156 W22 Y61 E116 M118 Q154
BS03 BGC E N22 W24 Y63 N20 W22 Y61
BS04 BGC E Y9 W113 Y7 W111
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008810 cellulase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0030245 cellulose 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:5gm4, PDBe:5gm4, PDBj:5gm4
PDBsum5gm4
PubMed27470581
UniProtP22669|GUN_ASPAC Endoglucanase-1

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