Structure of PDB 3gg2 Chain A

Receptor sequence
>3gg2A (length=431) Species: 837 (Porphyromonas gingivalis) [Search protein sequence]
SLDIAVVGIGYVGLVSATCFAELGANVRCIDTDRNKIEQLNSGTIPIYEP
GLEKMIARNVKAGRLRFGTEIEQAVPEADIIFIAVGTPAGEDGSADMSYV
LDAARSIGRAMSRYILIVTKSTVPVGSYRLIRKAIQEELDKREVLIDFDI
ASNPEFLKEGNAIDDFMKPDRVVVGVDSDRARELITSLYKPMLLNNFRVL
FMDIASAEMTKYAANAMLATRISFMNDVANLCERVGADVSMVRLGIGSDS
RIGSKFLYPGCGYGGSCFPKDVKALIRTAEDNGYRMEVLEAVERVNEKQK
SILFDKFSTYYKGNVQGRCVAIWGLSFKPGTDDMREAPSLVLIEKLLEVG
CRVRVYDPVAMKEAQKRLGDKVEYTTDMYDAVRGAEALFHVTEWKEFRMP
DWSALSQAMAASLVIDGRNVYELPFTLLNIG
3D structure
PDB3gg2 Crystal structure of UDP-glucose 6-dehydrogenase from Porphyromonas gingivalis bound to product UDP-glucuronate
ChainA
Resolution1.7 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) T199 E236 K288 N292 C344 D348
Catalytic site (residue number reindexed from 1) T122 E159 K211 N215 C267 D271
Enzyme Commision number 1.1.1.22: UDP-glucose 6-dehydrogenase.
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 UGA A F233 L234 K235 E236 K288 N292 I299 F333 Y335 Y340 G341 C344 F345 F404 K405 F156 L157 K158 E159 K211 N215 I222 F256 Y258 Y263 G264 C267 F268 F327 K328
BS02 UGA A M244 K245 L270 L271 N272 R275 M167 K168 L193 L194 N195 R198
BS03 UGA A F333 Y335 E470 F256 Y258 E393
Gene Ontology
Molecular Function
GO:0003979 UDP-glucose 6-dehydrogenase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0051287 NAD binding
Biological Process
GO:0000271 polysaccharide biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3gg2, PDBe:3gg2, PDBj:3gg2
PDBsum3gg2
PubMed
UniProtQ7MVC7

[Back to BioLiP]