Structure of PDB 3thc Chain D

Receptor sequence
>3thcD (length=602) Species: 9606 (Homo sapiens) [Search protein sequence]
QRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLN
AIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICA
EWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGG
PVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFL
KCGALQGLYTTVDFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWG
QPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQP
TSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVT
LEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRTTLPQDCSN
PAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVE
NMGRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWN
YTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPAR
GPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIG
SS
3D structure
PDB3thc Crystal structure of human beta-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases
ChainD
Resolution1.8 Å
3D
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
Enzyme Commision number 3.2.1.23: beta-galactosidase.
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 GAL D Y83 C127 A128 E129 N187 E188 E268 Y270 W273 L274 Y306 Y333 Y55 C99 A100 E101 N159 E160 E240 Y242 W245 L246 Y278 Y305
BS02 SO4 D R351 Q355 R323 Q327
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016936 galactoside binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0019388 galactose catabolic process
GO:0030200 heparan sulfate proteoglycan catabolic process
GO:0042340 keratan sulfate catabolic process
GO:0046479 glycosphingolipid catabolic process
GO:0051413 response to cortisone
GO:1904016 response to Thyroglobulin triiodothyronine
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005764 lysosome
GO:0005773 vacuole
GO:0005794 Golgi apparatus
GO:0035578 azurophil granule lumen
GO:0043202 lysosomal lumen
GO:0043231 intracellular membrane-bounded organelle
GO:0048471 perinuclear region of cytoplasm
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3thc, PDBe:3thc, PDBj:3thc
PDBsum3thc
PubMed22128166
UniProtP16278|BGAL_HUMAN Beta-galactosidase (Gene Name=GLB1)

[Back to BioLiP]