Structure of PDB 3lmy Chain A

Receptor sequence
>3lmyA (length=479) Species: 9606 (Homo sapiens) [Search protein sequence]
PALWPLPLSVKMTPNLLHLAPENFYISHSPNSTAGPSCTLLEEAFRRYHG
YIFTQVQQLLVSITLQSECDAFPNISSDESYTLLVKEPVAVLKANRVWGA
LRGLETFSQLVYQDSYGTFTINESTIIDSPRFSHRGILIDTSRHYLPVKI
ILKTLDAMAFNKFNVLHWHIVDDQSFPYQSITFPELSNKGSYSLSHVYTP
NDVRMVIEYARLRGIRVLPEFDTPGHTLSWGKGQKDLLTPCYSDSFGPIN
PTLNTTYSFLTTFFKEISEVFPDQFIHLGGDEVEFKCWESNPKIQDFMRQ
KGFGTDFKKLESFYIQKVLDIIATINKGSIVWQEVFDDKAKLAPGTIVEV
WKDSAYPEELSRVTASGFPVILSAPWYLDLISYGQDWRKYYKVEPLDFGG
TQKQKQLFIGGEACLWGEYVDATNLTPRLWPRASAVGERLWSSKDVRDMD
DAYDRLTRHRCRMVERGIAAQPLYAGYCN
3D structure
PDB3lmy The Crystal Structure of beta-hexosaminidase B in complex with Pyrimethamine
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D354 E355
Catalytic site (residue number reindexed from 1) D281 E282
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 CP6 A R211 H294 D354 W424 Y450 L453 W489 E491 R143 H226 D281 W351 Y377 L380 W416 E418 BindingDB: IC50=9100nM
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:3lmy, PDBe:3lmy, PDBj:3lmy
PDBsum3lmy
PubMed
UniProtP07686|HEXB_HUMAN Beta-hexosaminidase subunit beta (Gene Name=HEXB)

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