Structure of PDB 3exs Chain D

Receptor sequence
>3exsD (length=218) Species: 1309 (Streptococcus mutans) [Search protein sequence]
QLPNLQVALDHSNLKGAITAAVSVGNEVDVIEAGTVCLLQVGSELVEVLR
SLFPDKIIVADTKCADAGGTVAKNNAVRGADWMTCICSATIPTMKAARKA
IEDINPDKGEIQVELYGDWTYDQAQQWLDAGISQAIYHQSRDALLAGETW
GEKDLNKVKKLIEMGFRVSVTGGLSVDTLKLFEGVDVFTFIAGRGITEAK
NPAGAARAFKDEIKRIWG
3D structure
PDB3exs Open-closed conformational change revealed by the crystal structures of 3-keto-L-gulonate 6-phosphate decarboxylase from Streptococcus mutans
ChainD
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T38 V39 K66 D69 A70 V74 E117 H141 R144
Catalytic site (residue number reindexed from 1) T35 V36 K63 D66 A67 V71 E114 H138 R141
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 D D13 H141 T174 G176 G196 R197 D10 H138 T171 G173 G193 R194
Gene Ontology
Molecular Function
GO:0004590 orotidine-5'-phosphate decarboxylase activity
GO:0016829 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:0006730 one-carbon metabolic process
GO:0019854 L-ascorbic acid catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3exs, PDBe:3exs, PDBj:3exs
PDBsum3exs
PubMed19222992
UniProtQ93DA8

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