Structure of PDB 4gpn Chain B

Receptor sequence
>4gpnB (length=476) Species: 210007 (Streptococcus mutans UA159) [Search protein sequence]
SKLPENFLWGGAVAAHQLEGGWQEGGKGISVADVMTAGRHGVAREITAGV
LEGKYYPNHEAIDFYHHYKEDVKLFAEMGFKCFRTSIAWTRIFPKGDEAE
PNEAGLQFYDDLFDECLKYGIEPVVTLSHFELPYHLVTEYGGFTNRKVID
FFVHFAEVCFRRYKDKVKYWMTFNEINNQANYQEDFAPFTNSGIVYKEGD
DREAIMYQAAHYELVASARAVKIGHAINPNLNIGCMVAMCPIYPATCNPK
DILMAQKAMQKRYYFADVHVHGFYPEHIFKYWERKAIKVDFTERDKKDLF
EGTVDYIGFSYYMSFVIDAHRENNPYYDYLETEDLVKNPYVKASDWDWQI
DPQGLRYALNWFTDMYHLPLFIVQNGFGAIDQVEADGMVHDDYRIDYLGA
HIKEMIKAVDEDGVELMGYTPWGCIDLVSAGTGEMRKRYGFIYVDKDDEG
KGTLKRSPKLSFNWYKEVIASNGDDI
3D structure
PDB4gpn GH1-family 6-P-beta-glucosidases from human microbiome lactic acid bacteria.
ChainB
Resolution2.291 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R85 H130 E176 N179 S311 Y313 Q375
Catalytic site (residue number reindexed from 1) R84 H129 E175 N178 S310 Y312 Q374
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 BGC B E176 W349 E175 W348
BS02 BG6 B Q18 H130 F131 E176 Y313 W349 Q375 W423 S430 A431 G432 K438 Y440 Q17 H129 F130 E175 Y312 W348 Q374 W422 S429 A430 G431 K437 Y439
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:4gpn, PDBe:4gpn, PDBj:4gpn
PDBsum4gpn
PubMed23519420
UniProtQ8DT00

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