Structure of PDB 1u7z Chain C

Receptor sequence
>1u7zC (length=219) Species: 562 (Escherichia coli) [Search protein sequence]
SPVNDLKHLNIMITAGPTREPLDPVRYISDHSSGKMGFAIAAAAARRGAN
VTLVSGPVSLPTPPFVKRVDVMTALEMEAAVNASVQQQNIFIGCAAVADY
RAATVAPEKIKKELTIKMVKNPDIVAGVAALKDHRPYVVGFAAETNNVEE
YARQKRIRKNLDLICANDVSQPTQGFNSDNNALHLFWQDGDKVLPLERKE
LLGQLLLDEIVTRYDEKNR
3D structure
PDB1u7z Structural Basis of CTP-Dependent Peptide Bond Formation in Coenzyme A Biosynthesis Catalyzed by Escherichia coli PPC Synthetase
ChainC
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) D30
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 C S212 S213 G214 K215 M216 G273 C274 A275 A276 V277 D309 I310 V311 F327 A329 K341 K345 N353 F362 K385 S32 S33 G34 K35 M36 G93 C94 A95 A96 V97 D123 I124 V125 F141 A143 K155 K159 N167 F176 K199
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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