Structure of PDB 1q6r Chain A

Receptor sequence
>1q6rA (length=214) Species: 562 (Escherichia coli) [Search protein sequence]
SLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLK
ALYPHKIVLADAKIADAGKILSRMCFEANADWVTVICCADINTAKGALDV
AKEFNGDVQIELTGYWTWEQAQQWRDAGIGQVVYHRSRDAQAAGVAWGEA
DITAIKRLSDMGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPV
EAARQFKRSIAELW
3D structure
PDB1q6r 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
ChainA
Resolution1.76 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 LX1 A D11 H136 T169 G171 G191 R192 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

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Molecular Function
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Biological Process
External links
PDB RCSB:1q6r, PDBe:1q6r, PDBj:1q6r
PDBsum1q6r
PubMed14567674
UniProtP39304|ULAD_ECOLI 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (Gene Name=ulaD)

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