Structure of PDB 1ksd Chain A

Receptor sequence
>1ksdA (length=433) Species: 62960 (Nasutitermes takasagoensis) [Search protein sequence]
MAYDYKQVLRDSLLFYEAQRSGRLPADQKVTWRKDSALNDQGDQGQDLTG
GYFDAGDFVKFGFPMAYTATVLAWGLIDFEAGYSSAGALDDGRKAVKWAT
DYFIKAHTSQNEFYGQVGQGDADHAFWGRPEDMTMARPAYKIDTSRPGSD
LAGETAAALAAASIVFRNVDGTYSNNLLTHARQLFDFANNYRGKYSDSIT
DARNFYASADYRDELVWAAAWLYRATNDNTYLNTAESLYDEFGLQNWGGG
LNWDSKVSGVQVLLAKLTNKQAYKDTVQSYVNYLINNQQKTPKGLLYIDM
WGTLRHAANAAFIMLEAAELGLSASSYRQFAQTQIDYALGDGGRSFVCGF
GSNPPTRPHHRSSSCPPAPATCDWNTFNSPDPNYHVLSGALVGGPDQNDN
YVDDRSDYVHNEVATDYNAGFQSALAALVALGY
3D structure
PDB1ksd Structure of an endoglucanase from termite, Nasutitermes takasagoensis.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D54 D57 Y206 E412
Catalytic site (residue number reindexed from 1) D54 D57 Y206 E412
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 CA A D210 D213 E214 D254 D210 D213 E214 D254
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
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Biological Process
External links
PDB RCSB:1ksd, PDBe:1ksd, PDBj:1ksd
PDBsum1ksd
PubMed11914490
UniProtO77044

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