Structure of PDB 1dlj Chain A

Receptor sequence

>1dljA (length=402) Species: 1314 (Streptococcus pyogenes)

MKIAVAGSGYVGLSLGVLLSLQNEVTIVDILPSKVDKINNGLSPIQDEYI
EYYLKSKQLSIKATLDSKAAYKEAELVIIATPTNYNSRINYFDTQHVETV
IKEVLSVNSHATLIIKSTIPIGFITEMRQKFQTDRIIFSPEFLRESKALY
DNLYPSRIIVSCEENDSPKVKADAEKFALLLKSAAKKNNVPVLIMGASEA
EAVKLFANTYLALRVAYFNELDTYAESRKLNSHMIIQGISYDDRIGMHYN
NPSFGYGGYSLPKDTKQLLANYNNIPQTLIEAIVSSNNVRKSYIAKQIIN
VLKEQESPVKVVGVYRLIMKSNSDNFRESAIKDVIDILKSKDIKIIIYEP
MLNKLESEDQSVLVNDLENFKKQANIIVTNRYDNELQDVKNKVYSRDIFG
RD

3D structure

• PDB: 1dlj The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation.
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T118 E145 K204 N208 S260 D264
• Catalytic site (residue number reindexed from 1): T118 E145 K204 N208 S260 D264
• 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	NAI	A	G7 G9 Y10 V11 D29 I30 L31 K34 T81 P82 T83 S117 E141 L143 E145 Y259 K263 R327	G7 G9 Y10 V11 D29 I30 L31 K34 T81 P82 T83 S117 E141 L143 E145 Y259 K263 R327
BS02	UGA	A	F142 L143 R144 E145 K204 V215 Y249 N251 S253 G257 S260 M319 K320 R381 D402	F142 L143 R144 E145 K204 V215 Y249 N251 S253 G257 S260 M319 K320 R381 D402

Gene Ontology

Molecular Function

• GO:0003979 UDP-glucose 6-dehydrogenase activity
• GO:0016491 oxidoreductase 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
• GO:0006065 UDP-glucuronate biosynthetic process

External links

• PDB: RCSB:1dlj, PDBe:1dlj, PDBj:1dlj
• PDBsum: 1dlj
• PubMed: 10841783
• UniProt: P0C0F4|UDG_STRPY UDP-glucose 6-dehydrogenase (Gene Name=hasB)