Structure of PDB 2okx Chain A Binding Site BS01

Receptor Information
>2okx Chain A (length=954) Species: 84635 (Bacillus sp. GL1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GRNWNASWIWGGQEESPRNEWRCFRGSFDAPASVEGPAMLHITADSRYVL
FVNGEQVGRGPVRSWPKEQFYDSYDIGGQLRPGVRNTIAVLVLHFGVSNF
YYLRGRGGLIAEIEADGRTLAATDAAWRTERLGGQRSNSPRMACQQGFGE
VIDARELAEDWALPAFDDGGWAQARSIGPAGTAPWTSLVPRDIPFLTEEK
LYPASIQSLSRVKAPKYAAALDLRNQMVPESVNHANPVSYCGYVATILTL
ETSGVVTLGFPTGVRGSGVWVDGVLQTEWTGVQPERYYSLNLAAGEHLVL
VDITSSDHGGSSHFAIDSEAAFTLRSPAGDNGVPLATIGTFDQSEYIDHR
PGRRMQTDHPDYRALPEAAPTAAALEAFASWVKPFEPSLYTEENVFGSNV
WRTLAERRAVPRSVLNAILPVPEPGVLPVFEDGDCELVIDLGAERSGFIG
FELEAPAGTIIDAYGVEYMREGYTQHTYGLDNTFRYICREGRQSYVSPVR
RGFRYLFLTVRGNSAPVKLHEIYIRQSTYPVAEQGSFRCSDALLNATWEI
SRHTTRLCMEDTFVDCPSYEQVFWVGDSRNEALVNYYVFGETEIVERCLN
LVPGSADETPLYLDQVPSAWSSVIPNWTFFWILACREYAAHTGNEAFAAR
IWPAVKHTLTHYLEHIDDSGLLNMAGWNLLDWAPIDQPNEGIVTHQNLFL
VKALRDSRALAAAAGATEEADAFAARADLLAETINAVLWDEEKRAYIDCI
HADGRRSDVYSMQTQVVAYLCGVAQGEREAVIEGYLSSPPPAFVQIGSPF
MSFFYYEALEKAGRQTLMLDDIRRNYGQMLRYDATTCWEMYPNFAENRSN
PDMLTRSHCHAWSAAPGYFLGSSILGVKRGADGWRTVDIAPQPCDLTWAE
GVVPLPQGGHIAVSWEFVSAGKLKLRIEAPEDIEVNVTLPEGIEGEVTQV
KYMS
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 chain2okx Chain A Residue 4001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2okx Crystal Structure of Glycoside Hydrolase Family 78 alpha-L-Rhamnosidase from Bacillus sp. GL1
Resolution1.9 Å
Binding residue
(original residue number in PDB)		V423 H522
Binding residue
(residue number reindexed from 1)		V421 H520
Annotation score1
Enzymatic activity
Enzyme Commision number 3.2.1.40: alpha-L-rhamnosidase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016787 hydrolase activity
GO:0030596 alpha-L-rhamnosidase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2okx, PDBe:2okx, PDBj:2okx
PDBsum2okx
PubMed17936784
UniProtQ93RE7

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