Structure of PDB 3gg2 Chain C

Receptor sequence
>3gg2C (length=420) Species: 837 (Porphyromonas gingivalis) [Search protein sequence]
LDIAVVGIGYVGLVSATCFAELGANVRCIDTDRNKIEQLNSIYEPGLEKM
IARNVKAGRLRFGTEIEQAVPEADIIFIAVGTPADGSADMSYVLDAARSI
GRAMSRYILIVTKSTVPVGSYRLIRKAIQEELDKREVLIDFDIASNPEFL
KEGNAIDDFMKPDRVVVGVDSDRARELITSLYKPMRVLFMDIASAEMTKY
AANAMLATRISFMNDVANLCERVGADVSMVRLGIGSDSRIGSKFLYPGCG
YGGSCFPKDVKALIRTAEDNGYRMEVLEAVERVNEKQKSILFDKFSTYYK
GNVQGRCVAIWGLSFKPGTDDMREAPSLVLIEKLLEVGCRVRVYDPVAMK
EAQKRLGDKVEYTTDMYDAVRGAEALFHVTEWKEFRMPDWSALSQAMAAS
LVIDGRNVYELPDFTLLNIG
3D structure
PDB3gg2 Crystal structure of UDP-glucose 6-dehydrogenase from Porphyromonas gingivalis bound to product UDP-glucuronate
ChainC
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T199 E236 K288 N292 C344 D348
Catalytic site (residue number reindexed from 1) T115 E152 K199 N203 C255 D259
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 C Y88 F233 L234 K235 K288 N292 I299 F333 Y335 Y340 G341 C344 F345 F404 K405 R495 Y10 F149 L150 K151 K199 N203 I210 F244 Y246 Y251 G252 C255 F256 F315 K316 R406
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3gg2, PDBe:3gg2, PDBj:3gg2
PDBsum3gg2
PubMed
UniProtQ7MVC7

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