Structure of PDB 5bxp Chain B

Receptor sequence
>5bxpB (length=636) Species: 398514 (Bifidobacterium bifidum JCM 1254) [Search protein sequence]
HHSSGLVPRGSHMGYSATAPVNLTRPATVPSMDGWTDGTGAWTLGEGTRV
VSSDALAARAQSLASELTKFTDVDIKAATGSATGKDISLTLDASKKAELG
DEGFKLNIGSKGLEVIGATDIGVFYGTRSVSQMLRQGQLTLPAGTVATKP
KYKERGATLCACQINISTDWIDRFLSDMADLRLNYVLLEMKLKPEEDNTK
KAATWSYYTRDDVKKFVKKANNYGIDVIPEINSPGHMNVWLENYPEYQLA
DNSGRKDPNKLDISNPEAVKFYKTLIDEYDGVFTTKYWHMGADEYMIGTS
FDNYSKLKTFAEKQYGAGATPNDAFTGFINDIDKYVKAKGKQLRIWNDGI
VNTKNVSLNKDIVIEYWYGAGRKPQELVQDGYTLMNATQALYWSRSAQVY
KVNAARLYNNNWNVGTFDGGRQIDKNYDKLTGAKVSIWPDSSYFQTENEV
EKEIFDGMRFISQMTWSDSRPWATWNDMKADIDKIGYPLDIREYDYTPVD
AGIYDIPQLKSISKGPWELITTPDGYYQMKDTVSGKCLALFTGSKHLDVV
TQVGARPELRNCADVSVGQDQRNTANERNTQKWQIRADKDGKYTISPALT
QQRLAIATGNEQNIDLETHRPAAGTVAQFPADLVSD
3D structure
PDB5bxp Gaining insight into the catalysis by GH20 lacto-N-biosidase using small molecule inhibitors and structural analysis
ChainB
Resolution1.7 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 LOG B D320 E321 W394 Y419 Y427 W465 D467 D293 E294 W367 Y392 Y400 W438 D440
BS02 GAL B C187 C189 E216 N259 H263 P466 D467 C160 C162 E189 N232 H236 P439 D440
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5bxp, PDBe:5bxp, PDBj:5bxp
PDBsum5bxp
PubMed26312778
UniProtB3TLD6|LNBB_BIFB1 Lacto-N-biosidase (Gene Name=lnbB)

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