Structure of PDB 1xbz Chain A

Receptor sequence

>1xbzA (length=210) Species: 562 (Escherichia coli)

LPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKA
LYPHKIVLADAKIADAGKILSRMCFEANADWVTVICCADINTAKGALDVA
KEFNGDVQIDLTGYWTWEQAQQWRDAGIGQVVYHRSVDAQVAWGEADITA
IKRLSDMGFKVTVAGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVEAAR
QFKRSIAELW

3D structure

• PDB: 1xbz 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: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T36 I37 K64 D67 A68 L72 D112 H136 V139
• Catalytic site (residue number reindexed from 1): T34 I35 K62 D65 A66 L70 D110 H134 V137
• 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	E31 D60
BS02	MG	A	E33 D62	E31 D60
BS03	LX1	A	A9 D11 H136 G171 G191 R192	A7 D9 H134 G166 G186 R187

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