Structure of PDB 1rzm Chain A

Receptor sequence
>1rzmA (length=338) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MIVVLKPGSTEEDIRKVVKLAESYNLKCHISKGQERTVIGIIGDDRYVVA
DKFESLDCVESVVRVLKPYKLVSREFHPEDTVIDLGDVKIGNGYFTIIAG
PCSVEGREMLMETAHFLSELGVKVLRGGAYKPRTSPYSFQGLGEKGLEYL
REAADKYGMYVVTEALGEDDLPKVAEYADIIQIGARNAQNFRLLSKAGSY
NKPVLLKRGFMNTIEEFLLSAEYIANSGNTKIILCERGIRTFEKATRNTL
DISAVPIIRKESHLPILVDPSHSGGRRDLVIPLSRAAIAVGAHGIIVEVH
PEPEKALSDGKQSLDFELFKELVQEMKKLADALGVKVN
3D structure
PDB1rzm Crystal Structure of the Reaction Complex of 3-Deoxy-d-arabino-heptulosonate-7-phosphate Synthase from Thermotoga maritima Refines the Catalytic Mechanism and Indicates a New Mechanism of Allosteric Regulation.
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.54: 3-deoxy-7-phosphoheptulonate synthase.
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 PEP A R126 Q182 G184 A185 K207 R237 H272 R126 Q182 G184 A185 K207 R237 H272
BS02 E4P A K131 P132 R133 T134 R186 K131 P132 R133 T134 R186
Gene Ontology
Molecular Function
GO:0003849 3-deoxy-7-phosphoheptulonate synthase activity
GO:0016740 transferase activity
GO:0016832 aldehyde-lyase activity
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009058 biosynthetic process
GO:0009073 aromatic amino acid family biosynthetic process
GO:0009423 chorismate biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1rzm, PDBe:1rzm, PDBj:1rzm
PDBsum1rzm
PubMed15276836
UniProtQ9WYH8|AROF_THEMA Phospho-2-dehydro-3-deoxyheptonate aldolase (Gene Name=aroF)

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