Structure of PDB 5zjp Chain B

Receptor sequence
>5zjpB (length=230) Species: 666 (Vibrio cholerae) [Search protein sequence]
KNFLNIEELKRFLNGQTVVSIQPVTGSPLDKTDFIVAMAIAVEQAGAKAL
RIEGVSNVAAVSAAVTIPIIGIVKRDLPDSPVRITPFVSDVDGLANAGAT
VIAFDATNRTRPESRERIAQAIKNTGCFAMADCSTFEDGLWANSQGVEIV
GSTLSGYVGDIEPTVPDFQLVKAFSEAGFFTMAEGRYNTPELAAKAIESG
AVAVTVGSALTRLEVVTQWFNNATQAAGER
3D structure
PDB5zjp Crystal structures and kinetic analyses of N-acetylmannosamine-6-phosphate 2-epimerases from Fusobacterium nucleatum and Vibrio cholerae
ChainB
Resolution2.66 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 5.1.3.9: N-acylglucosamine-6-phosphate 2-epimerase.
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 RFW B K76 Y159 E186 R188 G209 S210 R214 K74 Y157 E184 R186 G207 S208 R212
Gene Ontology
Molecular Function
GO:0003674 molecular_function
GO:0016853 isomerase activity
GO:0016857 racemase and epimerase activity, acting on carbohydrates and derivatives
GO:0047465 N-acylglucosamine-6-phosphate 2-epimerase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006051 N-acetylmannosamine metabolic process
GO:0006053 N-acetylmannosamine catabolic process
GO:0008150 biological_process
GO:0019262 N-acetylneuraminate catabolic process
Cellular Component
GO:0005575 cellular_component
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:5zjp, PDBe:5zjp, PDBj:5zjp
PDBsum5zjp
PubMed29969107
UniProtQ9KR62|NANE_VIBCH Putative N-acetylmannosamine-6-phosphate 2-epimerase (Gene Name=nanE)

[Back to BioLiP]