Structure of PDB 5bxs Chain A

Receptor sequence
>5bxsA (length=633) Species: 398514 (Bifidobacterium bifidum JCM 1254) [Search protein sequence]
SSGLVPRGSHMGYSATAPVNLTRPATVPSMDGWTDGTGAWTLGEGTRVVS
SDALAARAQSLASELTKFTDVDIKAATGSATGKDISLTLDASKKAELGDE
GFKLNIGSKGLEVIGATDIGVFYGTRSVSQMLRQGQLTLPAGTVATKPKY
KERGATLCACQINISTDWIDRFLSDMADLRLNYVLLEMKLKPEEDNTKKA
ATWSYYTRDDVKKFVKKANNYGIDVIPEINSPGHMNVWLENYPEYQLADN
SGRKDPNKLDISNPEAVKFYKTLIDEYDGVFTTKYWHMGADEYMIGTSFD
NYSKLKTFAEKQYGAGATPNDAFTGFINDIDKYVKAKGKQLRIWNDGIVN
TKNVSLNKDIVIEYWYGAGRKPQELVQDGYTLMNATQALYWSRSAQVYKV
NAARLYNNNWNVGTFDGGRQIDKNYDKLTGAKVSIWPDSSYFQTENEVEK
EIFDGMRFISQMTWSDSRPWATWNDMKADIDKIGYPLDIREYDYTPVDAG
IYDIPQLKSISKGPWELITTPDGYYQMKDTVSGKCLALFTGSKHLDVVTQ
VGARPELRNCADVSVGQDQRNTANERNTQKWQIRADKDGKYTISPALTQQ
RLAIATGNEQNIDLETHRPAAGTVAQFPADLVS
3D structure
PDB5bxs Gaining insight into the catalysis by GH20 lacto-N-biosidase using small molecule inhibitors and structural analysis
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.140: lacto-N-biosidase.
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 GAL A C189 E216 N259 H263 D320 P466 D467 C160 E187 N230 H234 D291 P437 D438
BS02 GC2 A D320 E321 W373 W394 Y419 Y427 W465 D467 D291 E292 W344 W365 Y390 Y398 W436 D438
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004563 beta-N-acetylhexosaminidase activity
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5bxs, PDBe:5bxs, PDBj:5bxs
PDBsum5bxs
PubMed26312778
UniProtB3TLD6|LNBB_BIFB1 Lacto-N-biosidase (Gene Name=lnbB)

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