Structure of PDB 2ckr Chain B Binding Site BS05

Receptor Information
>2ckr Chain B (length=305) Species: 2021 (Thermobifida fusca) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GTPVERYGKVQVCGTQLCDEHGNPVQLRGMSTHGIQWFDHCLTDSSLDAL
AYDWKADIIRLSMYIQEDGYETNPRGFTDRMHQLIDMATARGLYVIVDWH
ILTPGDPHYNLDRAKTFFAEIAQRHASKTNVLYEIANEPNGVSWASIKSY
AEEVIPVIRQRDPDSVIIVGTRGWSSLGVSEGSGPAEIAANPVNASNIMY
AFHFYAASHRDNYLNALREASELFPVFVTQFGTETYTGDGANDFQMADRY
IDLMAERKIGWTKWNYSDDFRSGAVFQPGTCASGGPWSGSSLKASGQWVR
SKLQS
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain2ckr Chain B Residue 1437 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2ckr The Crystal Structure of the Catalytic Domain of Thermobifida Fusca Endoglucanase Cel5A in Complex with Cellotetraose
Resolution1.77 Å
Binding residue
(original residue number in PDB)		D169 D173
Binding residue
(residue number reindexed from 1)		D44 D48
Annotation score4
Enzymatic activity
Enzyme Commision number 3.2.1.4: cellulase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2ckr, PDBe:2ckr, PDBj:2ckr
PDBsum2ckr
PubMed
UniProtQ01786|GUN5_THEFU Endoglucanase E-5 (Gene Name=celE)

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