Structure of PDB 4lk3 Chain C

Receptor sequence

>4lk3C (length=271) Species: 9606 (Homo sapiens)

RKRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHEN
FELINHDVVEPLYIEVDQIYHLASPASYNPIKTLKTNTIGTLNMLGLAKR
VGARLLLASTSEVYEGKAVAETMCYAYMKQEGVEVRVARIFNTFGPRMHM
NDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVS
SPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFLKPDIKKAKLMLGWEPVV
PLEEGLNKAIHYFRKELEYQA

3D structure

• PDB: 4lk3 Man o' war mutation in UDP-alpha-D-xylose synthase favors the abortive catalytic cycle and uncovers a latent potential for hexamer formation.
• Chain: C
• Resolution: 2.64 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T202 S203 E204 K235 R272
• Catalytic site (residue number reindexed from 1): T110 S111 E112 K117 R154
• Enzyme Commision number: 4.1.1.35: UDP-glucuronate decarboxylase.

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	NAD	C	G95 G98 F99 V100 D119 N120 T123 G124 D144 V145 L159 A160 S161 P162 T178 K235 I258 H267	G8 G11 F12 V13 D32 N33 T36 G37 D57 V58 L72 A73 S74 P75 T86 K117 I140 H149
BS02	UGA	C	P148 L149 Y150 N185 G188 L189 K191 R192 Y245 E249	P61 L62 Y63 N93 G96 L97 K99 R100 Y127 E131
BS03	POP	C	R272 V273	R154 V155

Gene Ontology

Molecular Function

• GO:0048040 UDP-glucuronate decarboxylase activity
• GO:0070403 NAD+ binding

Biological Process

• GO:0042732 D-xylose metabolic process

External links

• PDB: RCSB:4lk3, PDBe:4lk3, PDBj:4lk3
• PDBsum: 4lk3
• PubMed: 25521717
• UniProt: Q8NBZ7|UXS1_HUMAN UDP-glucuronic acid decarboxylase 1 (Gene Name=UXS1)