Structure of PDB 4mo2 Chain A

Receptor sequence
>4mo2A (length=363) Species: 192222 (Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819) [Search protein sequence]
MYDYLIVGSGLFGSIFAYEATEKGYTCLVVEQREHIGGNCYTENIKNINV
HKYGAHIFRTSDQNIWDYMNQFCEFNHFINSPIAIYKDEIYNLPFNMNTF
SKLWGIKTPNEARKIIEMQKQIIQHPPKNLEEQAISLVGTDVYEKLIKGY
TEKQWGRSCKDLPASIIRRLPVRYIYDNNYFNDPYQGIPKGGYTAIFDKM
LKKSKVILNTDFLKYKDKFKNKAKKIVFTGCIDAYYDYRYGALEYRSLKF
EHKILNLDNFQGVAVVNYTDKEIPYTRIIEHKHFEFGNTDTTVISEEYPL
EWIKGIEPYYPINDEKNQALYEKYKQLAKHESNVYFGGRLGEYRYYDMQD
VVRSALLFCKNEL
3D structure
PDB4mo2 Specificity of a UDP-GalNAc Pyranose-Furanose Mutase: A Potential Therapeutic Target for Campylobacter jejuni Infections.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) R169 R173 R246 R277 E297 Y345 D347
Catalytic site (residue number reindexed from 1) R169 R173 R246 R277 E297 Y345 D347
Enzyme Commision number 5.4.99.9: UDP-galactopyranose mutase.
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 FAD A V7 G8 G10 L11 E31 Q32 G38 A55 H56 I57 R59 D211 G230 G338 R339 Y345 Y346 D347 M348 V351 V7 G8 G10 L11 E31 Q32 G38 A55 H56 I57 R59 D211 G230 G338 R339 Y345 Y346 D347 M348 V351
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008767 UDP-galactopyranose mutase activity
GO:0016853 isomerase activity
GO:0050660 flavin adenine dinucleotide binding
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:4mo2, PDBe:4mo2, PDBj:4mo2
PDBsum4mo2
PubMed24302429
UniProtQ0P8H5

[Back to BioLiP]