Structure of PDB 3gg2 Chain B

Receptor sequence
>3gg2B (length=425) Species: 837 (Porphyromonas gingivalis) [Search protein sequence]
LDIAVVGIGYVGLVSATCFAELGANVRCIDTDRNKIEQLNSGTIPIYEPG
LEKMIARNVKAGRLRFGTEIEQAVPEADIIFIAVGTPAGEDGSADMSYVL
DAARSIGRAMSRYILIVTKSTVPVGSYRLIRKAIQEELDKREVLIDFDIA
SNPEFLKEGNAIDDFMKPDRVVVGVDSDRARELITSLYKPMLRVLFMDIA
SAEMTKYAANAMLATRISFMNDVANLCERVGADVSMVRLGIGSDSRIGSK
FLYPGCGYGGSCFPKDVKALIRTAEDNGYRMEVLEAVERVNEKQKSILFD
KFSTYYKGNVQGRCVAIWGLSFKPGTDDMREAPSLVLIEKLLEVGCRVRV
YDPVAMKEAQKRLGDKVEYTTDMYDAVRGAEALFHVTEWKEFRMPDWSAL
SQAMAASLVIDGRNVYELFTLLNIG
3D structure
PDB3gg2 Crystal structure of UDP-glucose 6-dehydrogenase from Porphyromonas gingivalis bound to product UDP-glucuronate
ChainB
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) T121 E158 K206 N210 C262 D266
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 B Y88 E232 F233 L234 K235 K288 I299 F333 Y335 Y340 C344 F345 F404 K405 Y10 E154 F155 L156 K157 K206 I217 F251 Y253 Y258 C262 F263 F322 K323
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]