Structure of PDB 4ipn Chain B

Receptor sequence
>4ipnB (length=457) Species: 170187 (Streptococcus pneumoniae TIGR4) [Search protein sequence]
TIFPDDFLWGGAVAANQVEGAYNEDGKGLSVQDVLPKGGLGEATENPTED
NLKLIGIDFYHKYKEDISLFSEMGFNVFRTSIAWSRIFPKGDEEEPNEAG
LKYYDELFDELHAHGIEPLVTLSHYETPLYLARKYHGWVDRRMIHFYEKF
ARTVLERYKDKVKYWLTFNEVNSVLELPFTSGGIDIPKENLSKQELYQAI
HHELVASSLVTKIAREINSEFKVGCMVLAMPAYPMTPNPKDVWATHEYEN
LNYLFSDVHVRGYYPNYAKRYFKENDINIEFAAEDAELLKNYTVDFLSFS
YYMSVTQSALPGLVNPYLESSEWGWQIDPIGLRIILNRYYDRYQIPLFIV
ENGLGAKDQLIKDELNNLTVQDDYRIQYMKEHLLQVAEALQDGVEIMGYT
SWGCIDCVSMSTAQLSKRYGLIYVDRNDDGSGTLNRYKKMSFTWYKEVIE
SNGESLF
3D structure
PDB4ipn Structural insights into the substrate specificity of a 6-phospho-&[beta]-glucosidase BglA-2 from Streptococcus pneumoniae TIGR4
ChainB
Resolution2.411 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R80 H125 E171 S174 S301 Y303 E364
Catalytic site (residue number reindexed from 1) R79 H124 E170 S173 S300 Y302 E351
Enzyme Commision number 3.2.1.86: 6-phospho-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 SGC B Y126 E171 S174 Y125 E170 S173
BS02 RTG B Q18 H125 N170 E364 W415 S422 M423 S424 Q17 H124 N169 E351 W402 S409 M410 S411
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0008706 6-phospho-beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0016052 carbohydrate 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:4ipn, PDBe:4ipn, PDBj:4ipn
PDBsum4ipn
PubMed23580646
UniProtA0A0H2UP35

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