Structure of PDB 1zlp Chain A

Receptor sequence
>1zlpA (length=284) Species: 3570 (Dianthus caryophyllus) [Search protein sequence]
KTTMHRLIEEHGSVLMPGVQDALSAAVVEKTGFHAAFVSGYSVSAAMLGL
PDFGLLTTTEVVEATRRITAAAPNLCVVVDGDTGGGGPLNVQRFIRELIS
AGAKGVFLEDQVWPKKCGHMRGKAVVPAEEHALKIAAAREAIGDSDFFLV
ARTDARAPHGLEEGIRRANLYKEAGADATFVEAPANVDELKEVSAKTKGL
RIANMIEGGKTPLHTPEEFKEMGFHLIAHSLTAVYATARALVNIMKILKE
KGTTRDDLDQMATFSEFNELISLESWYEMESKFK
3D structure
PDB1zlp Crystal Structure of the Petal Death Protein from Carnation Flower.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F64 S66 G67 Y68 D79 D107 D109 F134 E136 K142 C144 G145 H146 R179 E209 N231 T238 L240
Catalytic site (residue number reindexed from 1) F37 S39 G40 Y41 D52 D80 D82 F107 E109 K115 C117 G118 H119 R152 E182 N204 T211 L213
Enzyme Commision number 3.7.1.1: oxaloacetase.
4.1.3.-
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 MG A D107 K142 D80 K115
BS02 GAQ A C144 G145 R179 I233 C117 G118 R152 I206
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016740 transferase activity
GO:0016787 hydrolase activity
GO:0016829 lyase activity
GO:0030603 oxaloacetase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0047776 citramalate lyase activity
Biological Process
GO:0006107 oxaloacetate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1zlp, PDBe:1zlp, PDBj:1zlp
PDBsum1zlp
PubMed16342930
UniProtQ05957|PDP_DIACA Petal death protein (Gene Name=PDP)

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