Structure of PDB 5gm5 Chain A

Receptor sequence
>5gm5A (length=218) Species: 5053 (Aspergillus aculeatus) [Search protein sequence]
QLCDQYATYTGGVYTINNNLWGKDAGSGSQCTTVNSASSAGTSWSTKWNW
SGGENSVKSYANSGLTFNKKLVSQISQIPTTARWSYDNTGIRADVAYDLF
TAADINHVTWSGDYELMIWLARYGGVQPIGSQIATATVDGQTWELWYGAN
GSQKTYSFVAPTPITSFQGDVNDFFKYLTQNHGFPASSQYLITLQFGTAP
FTGGPATLSVSNWSASVQ
3D structure
PDB5gm5 Crystal structure and genetic modifications of FI-CMCase from Aspergillus aculeatus F-50
ChainA
Resolution1.73 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) E115 A199
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 A W24 Y63 D101 E118 M120 W21 Y60 D98 E115 M117
BS02 BGC A N22 W24 N19 W21
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:5gm5, PDBe:5gm5, PDBj:5gm5
PDBsum5gm5
PubMed27470581
UniProtP22669|GUN_ASPAC Endoglucanase-1

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