Structure of PDB 4c7f Chain B

Receptor sequence
>4c7fB (length=493) Species: 1902 (Streptomyces coelicolor) [Search protein sequence]
EPTPLDRVIPAPASVEPGGAPYRITRGTHIRVDDSREARRVGDYLADLLR
PATGYRLPVTSHGHGGIRLRLAEGPYGDEGYRLDSGREGVTITARKAAGL
FHGVQTLRQLLPAAVEKDSAQPGPWLVAGGTIEDTPRYAWRSAMLDVSRH
FFSVDEVKRYIDRVALYKYNKLHLHISDDQGWRLAIDSWPRLATYGGSTE
VGGGPGGHYTKADYEEIVRYAASRHLEVVPEIDMPGHTNAALASYAELNC
DGVAPPLYTGTKVGFSTLCVDKDVTYDFVDDVLGELAALTPGRYLHIGGD
EAHSTPQADFVAFMKRVQPIVAKYGKTVVGWHQLAGAEPVEGALVQYWGL
DRTSDAEKAQVAAAARNGTGLILSPADRTYLDMKYTKDTPLGLSWAGYVE
VRRSYDWDPAAYLPGAPAEAVRGVEAPLWTETLSDPDQLDFMAFPRLPGV
AELGWSPASTHDWDTYKVRLAGQAPHWEAMGIDYYRSPQVPWT
3D structure
PDB4c7f Structure and Activity of the Streptomyces Coelicolor A3(2) Beta-N-Acetylhexosaminidase Provides Further Insight Into Gh20 Family Catalysis and Inhibition.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D301 E302
Catalytic site (residue number reindexed from 1) D300 E301
Enzyme Commision number 3.2.1.52: beta-N-acetylhexosaminidase.
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 GC2 B R150 D301 E302 W332 W349 Y381 W396 W430 E432 R149 D300 E301 W331 W348 Y380 W395 W429 E431
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004563 beta-N-acetylhexosaminidase activity
GO:0016787 hydrolase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030203 glycosaminoglycan metabolic process
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4c7f, PDBe:4c7f, PDBj:4c7f
PDBsum4c7f
PubMed24559145
UniProtQ9L068

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