Structure of PDB 3bga Chain A

Receptor sequence
>3bgaA (length=1003) Species: 226186 (Bacteroides thetaiotaomicron VPI-5482) [Search protein sequence]
LPEWQSQYAVGLNKLAPHTYVWPYADASDIGKPGGYEQSPYYMSLNGKWK
FNWVKNPDNRPKDFYQPSYYTGGWADINVPGNWERQGYGTAIYVNETYEF
DDKMFNFKKNPPLVPFAENEVGSYRRTFKVPADWKGRRVVLCCEGVISFY
YVWVNGKLLGYNQGSKTAAEWDITDVLSEGENVVALEVYRWSSGAYLECQ
DMWRLSGIERDVYLYSTPKQYIADYKVSASLDKEKYKEGIFNLEVTVEGP
SATASSIAYTLKDASGKAVLQDAINIKSRGLSNFIAFDEKKIAEVKAWNA
EHPNLYTLVLELKDAQGKVTELTGCEVGFRTSEIKDGRFCINGVPVLVKG
TNRHEHSQLGRTVSKELMEQDIRLMKQHNINMVRNSHYPTHPYWYQLCDR
YGLYMIDEANIESHGMGYGPASLAKDSTWLTAHMDRTHRMYERSKNHPAI
VIWSQGNEAGNGINFERTYDWLKSVEKGRPVQYERAELNYNTDIYCRMYR
SVDEIKAYVGKKDIYRPFILCEYLHAMGNSCGGMKEYWEVFENEPMAQGG
CIWDWVDQNFREIDKDGKWYWTYGGDYGPEGIPSFGNFCGNGLVNAVREP
HPHLLEVKKIYQNIKATLSDRKNLKVCIKNWYDFSNLNEYILRWNVKGED
GTVLAEGTKEVDCEPHATVDVTLGAVKLPNTVREAYLNLSWSRKEATPLV
DTDWEVAYDQFVLAGNKNTTAYRPQKAGETAFVVDKNTGALSSLTLDGKE
LLAAPITLSLFRPATDNDNRDRNGARLWRKAGLNNLTQKVVSLKEEKTSA
TVRAEILNGKGQKVGMADFVYALDKNGALKVRTTFQPDTAIVKSMARLGL
TFRMADAYNQVSYLGRGDHETYIDRNQSGRIGLYDTTVERMFHYYATPQS
TANRTDVRWAKLTDQAGEGVFMESNRPFQFSIIPFSDVLLEKAHHINELE
RDGMITIHLDAEQAGVGTATCGPGVLPQYLVPVKKQSFEFTLYPVKEGHH
HHH
3D structure
PDB3bga Crystal structure analysis of beta-galactosidase from Bacteroides thetaiotaomicron VPI-5482.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D227 H380 H413 E438 H440 E484 Y525 E548 S610 F614 N617
Catalytic site (residue number reindexed from 1) D201 H354 H387 E412 H414 E458 Y499 E522 S584 F588 N591
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 MG A E438 H440 E484 E412 H414 E458
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005990 lactose catabolic process
GO:0009056 catabolic process
Cellular Component
GO:0009341 beta-galactosidase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3bga, PDBe:3bga, PDBj:3bga
PDBsum3bga
PubMed
UniProtQ8A799

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