Structure of PDB 1gon Chain A

Receptor sequence
>1gonA (length=447) Species: 1931 (Streptomyces sp.) [Search protein sequence]
ALTFPEGFLWGSATASYQIEGAAAEDGRTPSIWDTYARTPGRVRNGDTGD
VATDHYHRWREDVALMAELGLGAYRFSLAWPRIQPTGRGPALQKGLDFYR
RLADELLAKGIQPVATLYHWDLPQELENAGGWPERATAERFAEYAAIAAD
ALGDRVKTWTTLNEPWCSAFLGYGSGVHAPGRTDPVAALRAAHHLNLGHG
LAVQALRDRLPADAQCSVTLNIHHVRPLTDSDADADAVRRIDALANRVFT
GPMLQGAYPEDLVKDTAGLTDWSFVRDGDLRLAHQKLDFLGVNYYSPTLV
SAHSPWPGADRVAFHQPPGETTAMGWAVDPSGLYELLRRLSSDFPALPLV
ITENGAAFHDYADPEGNVNDPERIAYVRDHLAAVHRAIKDGSDVRGYFLW
SLLDNFEWAHGYSKRFGAVYVDYPTGTRIPKASARWYAEVARTGVLP
3D structure
PDB1gon Cloning, Overexpression, Crystallization and Preliminary X-Ray Analysis of a Family 1 Beta--Glucosidase from Streptomyces
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 SO4 A R204 F288 R290 R190 F274 R276
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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Cellular Component
External links
PDB RCSB:1gon, PDBe:1gon, PDBj:1gon
PDBsum1gon
PubMed
UniProtQ59976

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