Structure of PDB 7exw Chain A

Receptor sequence
>7exwA (length=644) Species: 565042 (Bifidobacterium longum subsp. longum JCM 1217) [Search protein sequence]
MNVTITSPFWKRRRDQIVESVIPYQWGVMNDEIDTTSKSHAVANLKVAAG
ELDDEFHGMVFQDSDVYKWLEEAAYALAYHPDPELKALCDRTVDLIARAQ
QSDGYLDTPYQIKSGVWADRPRFSLIQQSHEMYVMGHYIEAAVAYHQVTG
NEQALEVAKKMADCLDANFGPEEGKIHGADGHPEIELALAKLYEETGEKR
YLTLSQYLIDVRGQDPQFYAKQLKAMNGDNIFHGFYKPTYFQAAEPVRDQ
QTADGHAVRVGYLCTGVAHVGRLLGDQGLIDTAKRFWKNIVTRRMYVTGA
IGSTHVGESFTYDYDLPNDTMYGETCASVAMSMFAQQMLDLEPKGEYADV
LEKELFNGSIAGISLDGKQYYYVNALETTPDGLDNPDRHHVLSHRVDWFG
CACCPANIARLIASVDRYIYTERDGGKTVLSHQFIANTAEFASGLTVEQR
SNFPWDGHVEYTVSLPASATDSSVRFGLRIPGWSRGSYTLTVNGKPAVGS
LEDGFVYLVVNAGDTLEIALELDMSVKFVRANSRVRSDAGQVAVMRGPLV
YCAEQVDNPGDLWNYRLADGVTGADAAVAFQADLLGGVDTVDLPAVREHA
DEDDAPLYVDADEPRAGEPATLRLVPYYSWANREIGEMRVFQRR
3D structure
PDB7exw Substrate complex structure, active site labeling and catalytic role of the zinc ion in cysteine glycosidase.
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.185: non-reducing end beta-L-arabinofuranosidase.
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 09X A H142 Y145 H194 H270 E338 Y386 C415 C417 H130 Y133 H182 H256 E324 Y372 C401 C403
BS02 ZN A E338 C340 C417 C418 E324 C326 C403 C404
Gene Ontology
Molecular Function
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
GO:0102478 beta-L-arabinofuranosidase activity
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:7exw, PDBe:7exw, PDBj:7exw
PDBsum7exw
PubMed34735571
UniProtE8MGH8|HYBA1_BIFL2 Non-reducing end beta-L-arabinofuranosidase (Gene Name=hypBA1)

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