Structure of PDB 5oar Chain D

Receptor sequence
>5oarD (length=498) Species: 5062 (Aspergillus oryzae) [Search protein sequence]
SNSLQYVNVQVKDIEADLQHGVDESYTLDVEEDSDTITINAETVWGALHA
FTTLQQLVISDGHGGLIIEEPVNIKDSPLYPYRGIMLDTGRNFVSLPKIF
EQLEGMSLSKLNVLHWHIDDAQSWPIWVDVYPEMVKDAYSPHEIYSRNDV
RNIVNYARARGIRVIPEIDMPSHSSSGWKQVDPEMVTCTDSWWSNDDWPL
HTAVEPNPGQLDIIYNKTYEVVGNVYKELSDIFPDHWFHVGGDEIQPNCF
NFSTHVTKWFAEDPSRTYHDLAQYWVDHAVPIFQNYSQERRLVMWEDIAL
SADNAHDVPKNIVMQSWNNGLEYISNLTARGYDVIVSSSDFLYLDCGHGG
FVTNDPRYNVMANPDANTPNFNYGGNGGSWCAPYKTWQRIYDYDFTLNLT
ETQAKHIIGATAPLWGEQVDDINVSSMFWPRAAALAELVWSGNRDANGNK
RTTEMTQRILNFREYLVANGVQAQALVPKYCLQHPHACDLYRNQAAIQ
3D structure
PDB5oar Crystal structure of native beta-N-acetylhexosaminidase isolated from Aspergillus oryzae sheds light onto its substrate specificity, high stability, and regulation by propeptide.
ChainD
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D345 E346
Catalytic site (residue number reindexed from 1) D243 E244
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 TBR D N318 Y321 E322 N216 Y219 E220
BS02 NGT D R193 H275 E307 D345 E346 W419 Y445 W482 W517 R91 H173 E205 D243 E244 W317 Y343 W380 W415
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004563 beta-N-acetylhexosaminidase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5oar, PDBe:5oar, PDBj:5oar
PDBsum5oar
PubMed29239122
UniProtQ8J2T0|HEXA_ASPOZ Beta-hexosaminidase (Gene Name=nagA)

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