Structure of PDB 1gon Chain A Binding Site BS01
Receptor Information
>1gon Chain A (length=447) Species:
1931
(Streptomyces sp.) [
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ALTFPEGFLWGSATASYQIEGAAAEDGRTPSIWDTYARTPGRVRNGDTGD
VATDHYHRWREDVALMAELGLGAYRFSLAWPRIQPTGRGPALQKGLDFYR
RLADELLAKGIQPVATLYHWDLPQELENAGGWPERATAERFAEYAAIAAD
ALGDRVKTWTTLNEPWCSAFLGYGSGVHAPGRTDPVAALRAAHHLNLGHG
LAVQALRDRLPADAQCSVTLNIHHVRPLTDSDADADAVRRIDALANRVFT
GPMLQGAYPEDLVKDTAGLTDWSFVRDGDLRLAHQKLDFLGVNYYSPTLV
SAHSPWPGADRVAFHQPPGETTAMGWAVDPSGLYELLRRLSSDFPALPLV
ITENGAAFHDYADPEGNVNDPERIAYVRDHLAAVHRAIKDGSDVRGYFLW
SLLDNFEWAHGYSKRFGAVYVDYPTGTRIPKASARWYAEVARTGVLP
Ligand information
Ligand ID
SO4
InChI
InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
InChIKey
QAOWNCQODCNURD-UHFFFAOYSA-L
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
[O-]S(=O)(=O)[O-]
CACTVS 3.341
[O-][S]([O-])(=O)=O
ACDLabs 10.04
[O-]S([O-])(=O)=O
Formula
O4 S
Name
SULFATE ION
ChEMBL
DrugBank
DB14546
ZINC
PDB chain
1gon Chain A Residue 1481 [
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Receptor-Ligand Complex Structure
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PDB
1gon
Cloning, Overexpression, Crystallization and Preliminary X-Ray Analysis of a Family 1 Beta--Glucosidase from Streptomyces
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
R204 F288 R290
Binding residue
(residue number reindexed from 1)
R190 F274 R276
Annotation score
3
Enzymatic activity
Catalytic site (original residue number in PDB)
R89 H133 E178 C181 N307 Y309 E383
Catalytic site (residue number reindexed from 1)
R75 H119 E164 C167 N293 Y295 E353
Enzyme Commision number
3.2.1.21
: beta-glucosidase.
Gene Ontology
Molecular Function
GO:0004553
hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422
beta-glucosidase activity
GO:0016798
hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975
carbohydrate metabolic process
GO:0016052
carbohydrate catabolic process
GO:0030245
cellulose catabolic process
Cellular Component
GO:0005829
cytosol
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1gon
,
PDBe:1gon
,
PDBj:1gon
PDBsum
1gon
PubMed
UniProt
Q59976
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