Structure of PDB 4jkl Chain B

Receptor sequence
>4jklB (length=587) Species: 208435 (Streptococcus agalactiae 2603V/R) [Search protein sequence]
NAMLYPLLTKTRNTYDLGGIWNFKLGEHNPNELLPSDEVMVIPTSFNDLM
VSKEKRDYIGDFWYEKVIEVPKVSEDEEMVLRFGSVTHQAKIYVDGVLVG
EHKGGFTPFEVLVPECKYNNEKIKVSICANNVLDYTTLPVGNYSEIIQED
GSIKKKVRENFDFFNYAGVHRPLKLMIRPKNHIFDITITSRLSDDLQSAD
LHFLVETNQKVDEVRISVFDEDNKLVGETKDSRLFLSDVHLWEVLNAYLY
TARVEIFVDNQLQDVYEENFGLREIEVTNGQFLLNRKPIYFKGFGKHEDT
FINGRGLNEAANLMDLNLLKDMGANSFRTSHYPYSEEMMRLADRMGVLVI
DEVPAVGLFQNNGTWNLMQTKAAHEQAIQELVKRDKNHPSVVMWVVANEP
ASHEAGAHDYFEPLVKLYKDLDPQKRPVTLVNILMATPDRDQVMDLVDVV
CLNRYYGWYVDHGDLTNAEVGIRKELLEWQDKFPDKPIIITEYGADTLPG
LHSTWNIPYTEEFQCDFYEMSHRVFDGIPNLVGEQVWNFADFETNLMILR
VQGNHKGLFSRNRQPKQVVKEFKKRWMTIPHYHNKKN
3D structure
PDB4jkl Structure and Inhibition of Microbiome beta-Glucuronidases Essential to the Alleviation of Cancer Drug Toxicity.
ChainB
Resolution2.288 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D160 H295 H329 V354 L356 E408 Y464 E501 K565
Catalytic site (residue number reindexed from 1) D162 H297 H331 V356 L358 E399 Y455 E492 K556
Enzyme Commision number 3.2.1.31: beta-glucuronidase.
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 R463 Y465 R454 Y456
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0004566 beta-glucuronidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4jkl, PDBe:4jkl, PDBj:4jkl
PDBsum4jkl
PubMed26364932
UniProtQ8E0N2|BGLR_STRA5 Beta-glucuronidase (Gene Name=SAG0698)

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