Structure of PDB 2zox Chain A

Receptor sequence
>2zoxA (length=466) Species: 9606 (Homo sapiens) [Search protein sequence]
MAFPAGFGWAAATAAYQVEGGWDADGKGPCVWDTFTHQGGERVFKNQTGD
VACGSYTLWEEDLKCIKQLGLTHYRFSLSWSRLLPDGTTGFINQKGIDYY
NKIIDDLLKNGVTPIVTLYHFDLPQTLEDQGGWLSEAIIESFDKYAQFCF
STFGDRVKQWITINQANVLSVMSYDLGMFPPGIPHFGTGGYQAAHNLIKA
HARSWHSYDSLFRKKQKGMVSLSLFAVWLEPADPNSVSDQEAAKRAITFH
LDLFAKPIFIDGDYPEVVKSQIASMSQKQGYPSSRLPEFTEEEKKMIKGT
ADFFAVQYYTTRLIKYQENKKGELGILQDAEIEFFPDPSWKNVDWIYVVP
WGVCKLLKYIKDTYNNPVIYITENGFPQSDPAPLDDTQRWEYFRQTFQEL
FKAIQLDKVNLQVYCAWSLLDNFEWNQGYSSRFGLFHVDFEDPARPRVPY
TSAKEYAKIIRNNGLE
3D structure
PDB2zox Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R75 H120 Q165 V168 Q307 Y309 E373
Catalytic site (residue number reindexed from 1) R75 H120 Q165 V168 Q307 Y309 E373
Enzyme Commision number 3.2.1.21: beta-glucosidase.
3.2.1.45: glucosylceramidase.
3.2.1.46: galactosylceramidase.
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 GLC A Q17 H120 N164 Y309 E373 W417 E424 W425 F433 Q17 H120 N164 Y309 E373 W417 E424 W425 F433
BS02 PNG A S274 M275 K278 E318 K320 G322 E331 S274 M275 K278 E318 K320 G322 E331
BS03 MG A R75 S223 T372 R75 S223 T372
BS04 MG A T188 R285 T188 R285
Gene Ontology
Molecular Function
GO:0004336 galactosylceramidase activity
GO:0004348 glucosylceramidase activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0005515 protein binding
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0017042 glycosylceramidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006629 lipid metabolic process
GO:0006680 glucosylceramide catabolic process
GO:0006683 galactosylceramide catabolic process
GO:0009313 oligosaccharide catabolic process
GO:0016139 glycoside catabolic process
GO:0046477 glycosylceramide catabolic process
GO:0046479 glycosphingolipid catabolic process
GO:0050821 protein stabilization
GO:1901805 beta-glucoside catabolic process
GO:1903017 positive regulation of exo-alpha-sialidase activity
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:1902494 catalytic complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2zox, PDBe:2zox, PDBj:2zox
PDBsum2zox
PubMed18662675
UniProtQ9H227|GBA3_HUMAN Cytosolic beta-glucosidase (Gene Name=GBA3)

[Back to BioLiP]