Structure of PDB 2gk1 Chain I

Receptor sequence
>2gk1I (length=440) Species: 9606 (Homo sapiens) [Search protein sequence]
TLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRG
LETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILD
TLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQD
VKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFG
PVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDF
MRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTI
IQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYVVE
PLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNK
LTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQ
3D structure
PDB2gk1 Crystallographic Structure of Human beta-Hexosaminidase A: Interpretation of Tay-Sachs Mutations and Loss of G(M2) Ganglioside Hydrolysis.
ChainI
Resolution3.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D322 E323
Catalytic site (residue number reindexed from 1) D234 E235
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 I R178 H262 D322 E323 W373 W392 N423 W460 E462 R90 H174 D234 E235 W285 W304 N335 W372 E374 BindingDB: Ki=270nM
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

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:2gk1, PDBe:2gk1, PDBj:2gk1
PDBsum2gk1
PubMed16698036
UniProtP06865|HEXA_HUMAN Beta-hexosaminidase subunit alpha (Gene Name=HEXA)

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