Structure of PDB 1so4 Chain B

Receptor sequence

>1so4B (length=215) Species: 562 (Escherichia coli)

SLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLK
ALYPHKIVLADAAIADAGKILSRMCFEANADWVTVICCADINTAKGALDV
AKEFNGDVQIELTGYWTWEQAQQWRDAGIGQVVYHRSRDAQAAGVAWGEA
DITAIKRLSDMGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPV
EAARQFKRSIAELWG

3D structure

• PDB: 1so4 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: B
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T36 I37 A64 D67 A68 L72 E112 H136 R139
• Catalytic site (residue number reindexed from 1): T35 I36 A63 D66 A67 L71 E111 H135 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	B	E33 D62	E32 D61
BS02	TX4	B	A9 D11 H136 T169 G171 G191 R192	A8 D10 H135 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:1so4, PDBe:1so4, PDBj:1so4
• PDBsum: 1so4
• PubMed: 15157078
• UniProt: P39304|ULAD_ECOLI 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (Gene Name=ulaD)