Structure of PDB 4zh5 Chain B Binding Site BS04

Receptor Information
>4zh5 Chain B (length=425) Species: 6356 (Perinereis brevicirris) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QYNYREVLQKSILFYAAQRSGQLPGNNPIDWRDDSALDDQGNGGEDLTGG
WYDAGDHVKFGLPMAWTATTLIWGMIDLANGYGGDRNDAMQSVRWALDYF
MKCHVSDNELYGQVGDGHADHAYWGRPEEMTMDRPAWSLTPSAPGSDLAG
ETAAALAAGSILFSDSDASYANQLLDHARTIYDFAYNNRGIYSESIPNAA
DFYRSSAYEDELCWGALWLYRATGEQDYMDKANEFLPQGRPWAFSWDSKE
AGSLVLLTSFGNSNARAQLEDFLQSWFPGGDIHYTPLGLAWRDTWGSLRY
SANSAFIALLAAEEGVLTSQARTFARAQLDYMLGSTGRSFVVGFGTNPPL
RPHHRAASCPDMPASCGWDQASDPAPNPQVLDGALVGGPDDQDNYNDDRQ
DYISNEVACDYNAGFQGALAGILQL
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain4zh5 Chain B Residue 503 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4zh5 Biophysical and structural characterisation of the endoglucanase from Perinereis brevicirris
Resolution1.35 Å
Binding residue
(original residue number in PDB)		A215 D218 E219 D255
Binding residue
(residue number reindexed from 1)		A207 D210 E211 D247
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D61 D64 Y211 E414
Catalytic site (residue number reindexed from 1) D53 D56 Y203 E406
Enzyme Commision number 3.2.1.4: cellulase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4zh5, PDBe:4zh5, PDBj:4zh5
PDBsum4zh5
PubMed
UniProtF2Z7L1

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