Structure of PDB 3bga Chain B

Receptor sequence
>3bgaB (length=1000) Species: 226186 (Bacteroides thetaiotaomicron VPI-5482) [Search protein sequence]
LKQPLPEWQSQYAVGLNKLAPHTYVWPYADASDIGKPGGYEQSPYYMSLN
GKWKFNWVKNPDNRPKDFYQPSYYTGGWADINVPGNWERQGYGTAIYVNE
TYEFDDKMFNFKKNPPLVPFAENEVGSYRRTFKVPADWKGRRVVLCCEGV
ISFYYVWVNGKLLGYNQGSKTAAEWDITDVLSEGENVVALEVYRWSSGAY
LECQDMWRLSGIERDVYLYSTPKQYIADYKVSASLDKEKYKEGIFNLEVT
VEGPSATASSIAYTLKDASGKAVLQDAINIKSRGLSNFIAFDEKKIAEVK
AWNAEHPNLYTLVLELKDAQGKVTELTGCEVGFRTSEIKDGRFCINGVPV
LVKGTNRHEHSQLGRTVSKELMEQDIRLMKQHNINMVRNSHYPTHPYWYQ
LCDRYGLYMIDEANIESHGMGYGPASLAKDSTWLTAHMDRTHRMYERSKN
HPAIVIWSQGNEAGNGINFERTYDWLKSVEKGRPVQYERAELNYNTDIYC
RMYRSVDEIKAYVGKKDIYRPFILCEYLHAMGNSCGGMKEYWEVFENEPM
AQGGCIWDWVDQNFREIDKDGKWYWTYGGDYGPEGIPSFGNFCGNGLVNA
VREPHPHLLEVKKIYQNIKATLSDRKNLKVCIKNWYDFSNLNEYILRWNV
KGEDGTVLAEGTKEVDCEPHATVDVTLGAVKLPNTVREAYLNLSWSRKEA
TPLVDTDWEVAYDQFVLAGNKNTTAYRPQKAGETAFVVDKNTGALSSLTL
DGKELLAAPITLSLFRPATDNDNRDRNGARLWRKAGLNNLTQKVVSLKEE
KTSATVRAEILNGKGQKVGMADFVYALDKNGALKVRTTFQPDTAIVKSMA
RLGLTFRMADAYNQVSYLGRGDHETYIDRNQSGRIGLYDTTVERMFHYYA
TPQSTANRTDVRWAKLTDQAGEGVFMESNRPFQFSIIPFSDVLLEKAHHI
NELERDGMITIHLDAEQAGVGTATCGPGVLPQYLVPVKKQSFEFTLYPVK
3D structure
PDB3bga Crystal structure analysis of beta-galactosidase from Bacteroides thetaiotaomicron VPI-5482.
ChainB
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) D205 H358 H391 E416 H418 E462 Y503 E526 S588 F592 N595
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 B E438 H440 E484 E416 H418 E462
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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