Structure of PDB 1q6q Chain A

Receptor sequence

>1q6qA (length=213) Species: 562 (Escherichia coli)

SLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLK
ALYPHKIVLADAKIADAGKILSRMCFEANADWVTVICCADINTAKGALDV
AKEFNGDVQIELTGYWTWEQAQQWRDAGIGQVVYHRSRDAQAAVAWGEAD
ITAIKRLSDMGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVE
AARQFKRSIAELW

3D structure

• PDB: 1q6q Structural Evidence for a 1,2-Enediolate Intermediate in the Reaction Catalyzed by 3-Keto-l-Gulonate 6-Phosphate Decarboxylase, a Member of the Orotidine 5'-Monophosphate Decarboxylase Suprafamily
• Chain: A
• Resolution: 1.695 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T36 I37 K64 D67 A68 L72 E112 H136 R139
• Catalytic site (residue number reindexed from 1): T35 I36 K63 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	A	E33 D62	E32 D61
BS02	LXP	A	A9 D11 K64 H136 T169 G171 G191 R192	A8 D10 K63 H135 T167 G169 G189 R190

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:1q6q, PDBe:1q6q, PDBj:1q6q
• PDBsum: 1q6q
• PubMed: 14567674
• UniProt: P39304|ULAD_ECOLI 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (Gene Name=ulaD)