Structure of PDB 1clx Chain D Binding Site BS01

Receptor Information
>1clx Chain D (length=345) Species: 155077 (Cellvibrio japonicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GLASLADFPIGVAVAASGGNADIFTSSARQNIVRAEFNQITAENIMKMSY
MYSGSNFSFTNSDRLVSWAAQNGQTVHGHALVWHPSYQLPNWASDSNANF
RQDFARHIDTVAAHFAGQVKSWDVVNEALFDSADDPDGRGSANGYRQSVF
YRQFGGPEYIDEAFRRARAADPTAELYYNDFNTEENGAKTTALVNLVQRL
LNNGVPIDGVGFQMHVMNDYPSIANIRQAMQKIVALSPTLKIKITELDVR
LNNPYDGNSSNDYTNRNDCAVSCAGLDRQKARYKEIVQAYLEVVPPGRRG
GITVWGIADPDSWLYTHQNLPDWPLLFNDNLQPKPAYQGVVEALS
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 chain1clx Chain D Residue 348 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1clx Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8 A resolution.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		N253 D256 N258 N261 D262
Binding residue
(residue number reindexed from 1)		N253 D256 N258 N261 D262
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E127 N179 H215 E246 D248
Catalytic site (residue number reindexed from 1) E127 N179 H215 E246 D248
Enzyme Commision number 3.2.1.8: endo-1,4-beta-xylanase.
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:1clx, PDBe:1clx, PDBj:1clx
PDBsum1clx
PubMed15299710
UniProtP14768|XYNA_CELJU Endo-1,4-beta-xylanase A (Gene Name=xynA)

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