Structure of PDB 1xbv Chain A

Receptor sequence

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

LPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKA
LYPHKIVLADAKIADAGKILSRMCFEANADWVTVICCADINTAKGALDVA
KEFNGDVQIELTGYWTWEQAQQWRDAGIGQVVYHRSRDAQAAGVAWGEAD
ITAIKRLSDMGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVE
AARQFKRSIAELW

3D structure

• PDB: 1xbv Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase
• Chain: A
• Resolution: 1.66 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): T34 I35 K62 D65 A66 L70 E110 H134 R137
• 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	5RP	A	A9 D11 H136 T169 G171 G191 R192	A7 D9 H134 T167 G169 G189 R190
BS02	MG	A	E33 D62	E31 D60

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:1xbv, PDBe:1xbv, PDBj:1xbv
• PDBsum: 1xbv
• PubMed: 15697207
• UniProt: P39304|ULAD_ECOLI 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (Gene Name=ulaD)