Structure of PDB 5wzn Chain B

Receptor sequence
>5wznB (length=619) Species: 1681 (Bifidobacterium bifidum) [Search protein sequence]
MMQFTMSGTMLRFDETTLRFSFSRDGATWSGCDGIEPQLTREDRSFSFAG
AATVTHERIETGTGVGVRSVFAGFAGADYAFETYIWIERSSGDVLCEWVP
LREEPRIDRVLWPAPLSFDRADAHDVTLITHEQGVMIPNSWPTEVGTDAV
SFGGRFETAGGYMPWFAQLRSDGHAYIAICETPWNAGYDIDHPAGGPYTH
VGMWFEPSLGRMDYRRVVRYRLLDHADHTAICKTYRAYVNERGRLRTLAE
KAARNPSVRDLLGRSWVHVGIKTNVQPDSSFYDPAQPGKNDSLVTFAQRE
RQMRTLHEMGAGRLYLHLDGWAQPGYDNGHPDYLPACREAGGWKGMKSLI
DACHEQGDLFGTHDQYRDYYFAARTFDPRNAIRLADGTMPEHAMWAGGRQ
TYLCAELAPDYVRRNFSEIATHGIVLDCAYLDVFTCNEGDECSHPEHRMT
RRECYERRAECFEYLLAHGILTSSEEVSDWAVPSLVFCHYAPYDFQMRSP
DAPRHGIPVPLYNLVYHDCVIQPWMMDRVAGGDDYMLYALLNGGAPYLIR
DAAYAGMDGDMNNDIERCAVVAGLHRRVGMQELVRHDLVGGDPLVQRSVF
ADGTAVTCDFHAQTYEVAA
3D structure
PDB5wzn The first crystal structure of a family 129 glycoside hydrolase from a probiotic bacterium reveals critical residues and metal cofactors
ChainB
Resolution2.1 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.2.1.-
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 ZN B C407 C445 H450 C404 C442 H447
BS02 CA B H271 H320 D322 H366 H268 H317 D319 H363
Gene Ontology
Molecular Function
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033926 endo-alpha-N-acetylgalactosaminidase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:5wzn, PDBe:5wzn, PDBj:5wzn
PDBsum5wzn
PubMed28546425
UniProtG5ELM1

[Back to BioLiP]