Structure of PDB 1hp5 Chain A

Receptor sequence
>1hp5A (length=499) Species: 1922 (Streptomyces plicatus) [Search protein sequence]
DRKAPVRPTPLDRVIPAPASVDPGGAPYRITRGTHIRVDDSREARRVGDY
LADLLRPATGYRLPVTAHGHGGIRLRLAGGPYGDEGYRLDSGPAGVTITA
RKAAGLFHGVQTLRQLLPPAVEKDSAQPGPWLVAGGTIEDTPRYAWRSAM
LDVSRHFFGVDEVKRYIDRVARYKYNKLHLHLSDDQGWRIAIDSWPRLAT
YGGSTEVGGGPGGYYTKAEYKEIVRYAASRHLEVVPEIDMPGHTNAALAS
YAELNCDGVAPPLYTGTKVGFSSLCVDKDVTYDFVDDVIGELAALTPGRY
LHIGGDEAHSTPKADFVAFMKRVQPIVAKYGKTVVGWHQLAGAEPVEGAL
VQYWGLDRTGDAEKAEVAEAARNGTGLILSPADRTYLDMKYTKDTPLGLS
WAGYVEVQRSYDWDPAGYLPGAPADAVRGVEAPLWTETLSDPDQLDYMAF
PRLPGVAELGWSPASTHDWDTYKVRLAAQAPYWEAAGIDFYRSPQVPWT
3D structure
PDB1hp5 Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D313 E314
Catalytic site (residue number reindexed from 1) D306 E307
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 NGT A R162 H250 D313 E314 W344 W361 Y393 D395 W408 W442 E444 R155 H243 D306 E307 W337 W354 Y386 D388 W401 W435 E437 PDBbind-CN: -logKd/Ki=6.55,Ki=280nM
BindingDB: Ki=20000nM
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:1hp5, PDBe:1hp5, PDBj:1hp5
PDBsum1hp5
PubMed11124970
UniProtO85361

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