Structure of PDB 8ihy Chain A

Receptor sequence
>8ihyA (length=432) Species: 6396 (Eisenia fetida) [Search protein sequence]
YNYDEVLEKSILFYEAERSGDLPANNRIPYRGDSALGDQGNQGQDLTGGW
YDAGDHVKFGFPMAFATTTLAWGILEFRDGYEAAGQYNLALDSIRWTLNY
FLKAHVSDNEFYGQVGDANTDHAYWGRPEDMTMERPAWSISPSAPGSDLA
AETAAALAAGYLVFRDSDAAFANNLLAHSRTLYDFALNNRGIYSQSISNA
AGFYASSAYEDELAWGAAWLYRATEEQEYLDRAYEFGTTTNTAWAYDWNE
KIVGYQLLLTTSAGQTDFLPRVENFLRNWFPGGSVQYTPLGLAWLAQWGP
NRYAANAAFIALVSAKYNILASESEQFARSQIHYMLGDAGRSYVVGFGNN
PPQQPHHRSSSCPDEPAECDWDEFNQPGPNYQILYGALVGGPDQNDQFED
LRSDYIRNEVANDYNAGFQGAVAALRAIQLRD
3D structure
PDB8ihy A single mutation Asp43Arg was increased 2.5-fold the catalytic activity and maintained the stability of cold-adapted endo-1,4-beta glucanase (Ef-EG2) from Eisenia fetida.
ChainA
Resolution1.6 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 MG A D386 Q404 D364 Q382
BS02 CA A A230 D233 E234 N271 A208 D211 E212 N249
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008810 cellulase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030245 cellulose catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:8ihy, PDBe:8ihy, PDBj:8ihy
PDBsum8ihy
PubMed
UniProtI2FI81

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