Structure of PDB 1xbz Chain A Binding Site BS03

Receptor Information
>1xbz Chain A (length=210) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKA
LYPHKIVLADAKIADAGKILSRMCFEANADWVTVICCADINTAKGALDVA
KEFNGDVQIDLTGYWTWEQAQQWRDAGIGQVVYHRSVDAQVAWGEADITA
IKRLSDMGFKVTVAGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVEAAR
QFKRSIAELW
Ligand information
Ligand IDLX1
InChIInChI=1S/C5H13O7P/c1-3(6)5(8)4(7)2-12-13(9,10)11/h3-8H,2H2,1H3,(H2,9,10,11)/t3-,4+,5+/m1/s1
InChIKeyYPXGTKHZRCDZTL-WISUUJSJSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(O)OCC(O)C(O)C(O)C
OpenEye OEToolkits 1.5.0CC(C(C(COP(=O)(O)O)O)O)O
OpenEye OEToolkits 1.5.0C[C@H]([C@@H]([C@H](COP(=O)(O)O)O)O)O
CACTVS 3.341C[C@@H](O)[C@H](O)[C@@H](O)CO[P](O)(O)=O
CACTVS 3.341C[CH](O)[CH](O)[CH](O)CO[P](O)(O)=O
FormulaC5 H13 O7 P
NameL-XYLULOSE 5-PHOSPHATE
ChEMBL
DrugBank
ZINCZINC000006494205
PDB chain1xbz Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1xbz 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
Resolution1.8 Å
Binding residue
(original residue number in PDB)		A9 D11 H136 G171 G191 R192
Binding residue
(residue number reindexed from 1)		A7 D9 H134 G166 G186 R187
Annotation score2
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.
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1xbz, PDBe:1xbz, PDBj:1xbz
PDBsum1xbz
PubMed15697207
UniProtP39304|ULAD_ECOLI 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (Gene Name=ulaD)

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