Structure of PDB 5gm4 Chain G

Receptor sequence
>5gm4G (length=218) Species: 5053 (Aspergillus aculeatus) [Search protein sequence]
QLCDQYATYTGGVYTINNNLWGKDAGSGSQCTTVNSASSAGTSWSTKWNW
SGGENSVKSYANSGLTFNKKLVSQISQIPTTARWSYDNTGIRADVAYDLF
TAADINHVTWSGDYELMIWLARYGGVQPIGSQIATATVDGQTWELWYGAN
GSQKTYSFVAPTPITSFQGDVNDFFKYLTQNHGFPASSQYLITLQFGTAP
FTGGPATLSVSNWSASVQ
3D structure
PDB5gm4 Crystal structure and genetic modifications of FI-CMCase from Aspergillus aculeatus F-50
ChainG
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) 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 G D97 Q130 A202 F204 D94 Q127 A199 F201
BS02 BGC G W24 Y63 E118 M120 Q156 W21 Y60 E115 M117 Q153
BS03 BGC G N22 W24 N19 W21
BS04 BGC G Y9 W113 Y6 W110
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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