Structure of PDB 6mvf Chain A

Receptor sequence
>6mvfA (length=643) Species: 718252 (Faecalibacterium prausnitzii L2-6) [Search protein sequence]
NAMREIISLNEGWTLRFPKGERAAETVTLPHTWNAVDGMDGNGSYLRTTG
VYSRTFKKPVQPLTGGRVYVEVLAAALDATVKVNGTVATTHEGGFSIFRA
DITDLCRDGDNELTIEVSNEDTPSMYPASADFTFYGGLYRGVNLISVPNA
HFDLDYYGGPGIMVTPKPTADGGATFEIKSFVTNPDDSFTVMYSIEDPYG
CEVASAVRPSDNTAISIYVPDAELWSMDEPNLYTVVARLQRNNEAFDEIY
ANVGVRSYTVTPDGGFSINGEATPLRGVSRHQDKLYKGNALTVEDHYQDA
QIIKELGANTIRLAHYQHSQDFYDACDELGFAVWAEIPFISVFKSGKDAH
THVMEEMKELIIQNYNHPSILFWGISNEILIGGISQELVDTHHDLQKLCK
ELDPTRLTTIAHVSHTPTSGPMHRITDVESYNHYFGWYGGKIEQNGPWLD
KFHAENPDICLGISEYGCEGIINWHSNTPQCKDYSEEYQALYHEYMAQAF
EDRPWIWASHVWNMFDFGCAARSEGGVKGRNNKGLVTIDRKTRKDSFYVY
QAYWAKDPMVHIAGRRHAQRAGETTEVKVYSNQDTVTLYCNGKEVGTQTA
HRVFKFDVALDEGFNVLMAVADTVKDSITLEKVETEPACYTLP
3D structure
PDB6mvf Discovery and Characterization of FMN-Binding beta-Glucuronidases in the Human Gut Microbiome.
ChainA
Resolution2.55 Å
3D
structure
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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 FMN A D151 Y154 M161 F179 K356 I360 Y363 D153 Y156 M163 F181 K358 I362 Y365
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030245 cellulose catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6mvf, PDBe:6mvf, PDBj:6mvf
PDBsum6mvf
PubMed30658055
UniProtD4K3H3

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