Structure of PDB 5ljf Chain A

Receptor sequence
>5ljfA (length=321) Species: 77133 (uncultured bacterium) [Search protein sequence]
SVDLIGINVAGAEFTGGKLPGKHGTHYFFPPEGYFEYWSEQGIHTVRFPL
KWERLQPSLNAELDDVYASLVDDMLDQAKENDIKVILDVHNYARYRKKVI
GTEDVPVSAYQDLMERIAKRWQGHDALFAYDIMNAPYGSADKLWPAAAQA
GIDGVRKYDKKRPLLIEGASWSSAARWPRYADELLKLKDPADNMVFSAHV
YIDEDASGSYKKGPGKDFEPMIGVKRVEPFVNWLKEHGKKGHIGEFGIPN
DDERWLDAMDKLLAYLNENCIPINYWAAGPSWGNYKLSIEPKDGEKRPQV
ALLKKYAAKDNCSDFGPAKAE
3D structure
PDB5ljf Glycoside hydrolase family 5: structural snapshots highlighting the involvement of two conserved residues in catalysis.
ChainA
Resolution1.7344 Å
3D
structure
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Enzymatic activity
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 W171 R176 D205 W171 R176 D205
BS02 BGC A W171 Y201 A206 S207 W171 Y201 A206 S207
BS03 BGC A H90 N134 E245 W276 H90 N134 E245 W276
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:0009251 glucan catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5ljf, PDBe:5ljf, PDBj:5ljf
PDBsum5ljf
PubMed33559609
UniProtC1JI15

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