Structure of PDB 1a2n Chain A

Receptor sequence
>1a2nA (length=418) Species: 562 (Escherichia coli) [Search protein sequence]
MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDV
DTSMKLLSQLGAKVERNGSVHIDARDVNVFCAPYDLVKTMRASIWALGPL
VARFGQGQVSLPGGATIGARPVDLHISGLEQLGATIKLEEGYVKASVDGR
LKGAHIVMDKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLIT
LGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLVAAAISRGKII
CRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHP
AFPTDMQAQFTLLNLVAEGTGFITETVFENRFMHVPELSRMGAHAEIESN
TVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYE
RIEDKLRALGANIERVKG
3D structure
PDB1a2n Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound to the active site of the C115A mutant of MurA
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K22 N23 D49 A92 A115 R120 H299 D305 E325 L370 R371 R397
Catalytic site (residue number reindexed from 1) K22 N23 D49 A92 A115 R120 H299 D305 E325 L370 R371 R397
Enzyme Commision number 2.5.1.7: UDP-N-acetylglucosamine 1-carboxyvinyltransferase.
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 TET A K22 N23 R91 W95 R120 P121 V122 L124 S162 V163 G164 D305 V327 F328 R371 R397 K22 N23 R91 W95 R120 P121 V122 L124 S162 V163 G164 D305 V327 F328 R371 R397
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008760 UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
GO:0016740 transferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
Biological Process
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0019277 UDP-N-acetylgalactosamine biosynthetic process
GO:0051301 cell division
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1a2n, PDBe:1a2n, PDBj:1a2n
PDBsum1a2n
PubMed9485407
UniProtP0A749|MURA_ECOLI UDP-N-acetylglucosamine 1-carboxyvinyltransferase (Gene Name=murA)

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