Structure of PDB 8ihw Chain A

Receptor sequence
>8ihwA (length=433) Species: 6396 (Eisenia fetida) [Search protein sequence]
QYNYDEVLEKSILFYEAERSGRLPANNRIPYRGDSALGDQGNQGQDLTGG
WYDAGDHVKFGFPMAFATTTLAWGILEFRDGYEAAGQYNLALDSIRWTLN
YFLKAHVSDNEFYGQVGDANTDHAYWGRPEDMTMERPAWSISPSAPGSDL
AAETAAALAAGYLVFRDSDAAFANNLLAHSRTLYDFALNNRGIYSQSISN
AAGFYASSAYEDELAWGAAWLYRATEEQEYLDRAYEFGTTTNTAWAYDWN
EKIVGYQLLLTTSAGQTDFLPRVENFLRNWFPGGSVQYTPLGLAWLAQWG
PNRYAANAAFIALVSAKYNILASESEQFARSQIHYMLGDAGRSYVVGFGN
NPPQQPHHRSSSCPDQPAECDWDEFNQPGPNYQILYGALVGGPDQNDQFE
DLRSDYIRNEVANDYNAGFQGAVAALRAIQLRD
3D structure
PDB8ihw 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
Resolution1.7 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 D365 Q383
BS02 CA A A230 D233 E234 N271 A209 D212 E213 N250
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:8ihw, PDBe:8ihw, PDBj:8ihw
PDBsum8ihw
PubMed
UniProtI2FI81

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