Structure of PDB 1xbv Chain B Binding Site BS01

Receptor Information
>1xbv Chain B (length=215) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLK
ALYPHKIVLADAKIADAGKILSRMCFEANADWVTVICCADINTAKGALDV
AKEFNGDVQIELTGYWTWEQAQQWRDAGIGQVVYHRSRDAQAAGVAWGEA
DITAIKRLSDMGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPV
EAARQFKRSIAELWG
Ligand information
Ligand ID5RP
InChIInChI=1S/C5H11O8P/c6-1-3(7)5(9)4(8)2-13-14(10,11)12/h4-6,8-9H,1-2H2,(H2,10,11,12)/t4-,5+/m1/s1
InChIKeyFNZLKVNUWIIPSJ-UHNVWZDZSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OCC(=O)[C@H](O)[C@H](O)CO[P](O)(O)=O
OpenEye OEToolkits 1.5.0C(C(C(C(=O)CO)O)O)OP(=O)(O)O
CACTVS 3.341OCC(=O)[CH](O)[CH](O)CO[P](O)(O)=O
ACDLabs 10.04O=P(O)(O)OCC(O)C(O)C(=O)CO
OpenEye OEToolkits 1.5.0C([C@H]([C@H](C(=O)CO)O)O)OP(=O)(O)O
FormulaC5 H11 O8 P
NameRIBULOSE-5-PHOSPHATE
ChEMBL
DrugBank
ZINCZINC000001532567
PDB chain1xbv Chain B Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1xbv 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
Resolution1.66 Å
Binding residue
(original residue number in PDB)		D11 H136 T169 G171 G191 R192
Binding residue
(residue number reindexed from 1)		D10 H135 T168 G170 G190 R191
Annotation score5
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.
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:1xbv, PDBe:1xbv, PDBj:1xbv
PDBsum1xbv
PubMed15697207
UniProtP39304|ULAD_ECOLI 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (Gene Name=ulaD)

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