Structure of PDB 1kw1 Chain A

Receptor sequence
>1kw1A (length=213) Species: 562 (Escherichia coli) [Search protein sequence]
LPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKA
LYPHKIVLADAKIADAGKILSRMCFEANADWVTVICCADINTAKGALDVA
KEFNGDVQIELTGYWTWEQAQQWRDAGIGQVVYHRSRDAQAAGVAWGEAD
ITAIKRLSDMGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVE
AARQFKRSIAELW
3D structure
PDB1kw1 Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase.
ChainA
Resolution2.2 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) 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 MG A E33 D62 E31 D60
BS02 LG6 A A9 D11 T36 K64 H136 T169 G171 G191 R192 A7 D9 T34 K62 H134 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

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Molecular Function
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Biological Process
External links
PDB RCSB:1kw1, PDBe:1kw1, PDBj:1kw1
PDBsum1kw1
PubMed11900527
UniProtP39304|ULAD_ECOLI 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (Gene Name=ulaD)

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