Structure of PDB 1so3 Chain A

Receptor sequence

>1so3A (length=214) Species: 562 (Escherichia coli)

SLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLK
ALYPHKIVLADAKIADAGKILSRMCFEANADWVTVICCADINTAKGALDV
AKEFNGDVQIELTGYWTWEQAQQWRDAGIGQVVYARSRDAQAAGVAWGEA
DITAIKRLSDMGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPV
EAARQFKRSIAELW

3D structure

• PDB: 1so3 Evolution of Enzymatic Activities in the Orotidine 5'-Monophosphate Decarboxylase Suprafamily: Crystallographic Evidence for a Proton Relay System in the Active Site of 3-Keto-l-gulonate 6-Phosphate Decarboxylase(,)
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T36 I37 K64 D67 A68 L72 E112 A136 R139
• Catalytic site (residue number reindexed from 1): T35 I36 K63 D66 A67 L71 E111 A135 R138
• Enzyme Commision number: 4.1.1.85: 3-dehydro-L-gulonate-6-phosphate 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	MG	A	E33 D62	E32 D61
BS02	TX4	A	A9 D11 T169 G171 G191 R192	A8 D10 T168 G170 G190 R191

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004590 orotidine-5'-phosphate decarboxylase activity
• GO:0016831 carboxy-lyase activity
• GO:0033982 3-dehydro-L-gulonate-6-phosphate decarboxylase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
• GO:0019854 L-ascorbic acid catabolic process

External links

• PDB: RCSB:1so3, PDBe:1so3, PDBj:1so3
• PDBsum: 1so3
• PubMed: 15157078
• UniProt: P39304|ULAD_ECOLI 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (Gene Name=ulaD)