Structure of PDB 1u7z Chain A

Receptor sequence
>1u7zA (length=216) Species: 562 (Escherichia coli) [Search protein sequence]
VNDLKHLNIMITAGPTREPLDPVRYISDHSSGKMGFAIAAAAARRGANVT
LVSGPVSLPTPPFVKRVDVMTALEMEAAVNASVQQQNIFIGCAAVADYRA
ATVAPEKIDELTIKMVKNPDIVAGVAALKDHRPYVVGFAAETNNVEEYAR
QKRIRKNLDLICANDVSQPTQGFNSDNNALHLFWQDGDKVLPLERKELLG
QLLLDEIVTRYDEKNR
3D structure
PDB1u7z Structural Basis of CTP-Dependent Peptide Bond Formation in Coenzyme A Biosynthesis Catalyzed by Escherichia coli PPC Synthetase
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D210
Catalytic site (residue number reindexed from 1) D28
Enzyme Commision number 4.1.1.36: phosphopantothenoylcysteine decarboxylase.
6.3.2.5: phosphopantothenate--cysteine ligase (CTP).
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 PMT A S212 S213 G214 K215 M216 G273 C274 A275 A276 V277 D309 I310 V311 F327 A329 K341 K345 N353 F362 K385 S30 S31 G32 K33 M34 G91 C92 A93 A94 V95 D120 I121 V122 F138 A140 K152 K156 N164 F173 K196
Gene Ontology
Molecular Function
GO:0004632 phosphopantothenate--cysteine ligase activity
GO:0004633 phosphopantothenoylcysteine decarboxylase activity
GO:0010181 FMN binding
Biological Process
GO:0015937 coenzyme A biosynthetic process
GO:0015941 pantothenate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1u7z, PDBe:1u7z, PDBj:1u7z
PDBsum1u7z
PubMed15530362
UniProtP0ABQ0|COABC_ECOLI Coenzyme A biosynthesis bifunctional protein CoaBC (Gene Name=coaBC)

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