Structure of PDB 2jlc Chain A

Receptor sequence
>2jlcA (length=554) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MSVSAFNRRWAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHH
THFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPALIEAGLTGEKL
ILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVS
TIDHALGTLHAGGVHINCPFAEPLYMDDTGLSWQQRLGDWWQDDKPWLRE
APRLESEKQRDWFFWRQKRGVVVAGRMSAEEGKKVALWAQTLGWPLIGDV
LSQTGQPLPCADLWLGNAKATSELQQAQIVVQLGSSLTGKRLLQWQASCE
PEEYWIVDDIEGRLDPAHHRGRRLIANIADWLELHPAEKRQPWCVEIPRL
AEQAMQAVIARRDAFGEAQLAHRICDYLPEQGQLFVGNSLVVRLIDALSQ
LPAGYPVYSNRGASGIDGLLSTAAGVQRASGKPTLAIVGDLSALYDLNAL
ALLRQVSAPLVLIVVNNNGGQIFSLLPTPQSERERFYLMPQNVHFEHAAA
MFELKYHRPQNWQELETAFADAWRTPTTTVIEMVVNDTDGAQTLQQLLAQ
VSHL
3D structure
PDB2jlc Specificity and Reactivity in Menaquinone Biosynthesis: The Structure of Escherichia Coli Mend (2-Succinyl-5-Enolpyruvyl-6-Hydroxy-3-Cyclohexadiene-1-Carboxylate Synthase).
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A29 E55
Catalytic site (residue number reindexed from 1) A29 E55
Enzyme Commision number 2.2.1.9: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid 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 TPP A S391 L392 G417 I418 D419 G441 D442 L443 S444 Y447 N469 G471 G472 Q473 I474 S389 L390 G415 I416 D417 G439 D440 L441 S442 Y445 N467 G469 G470 Q471 I472
BS02 MN A D442 N469 G471 D440 N467 G469
BS03 TPP A P30 E55 P30 E55
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016740 transferase activity
GO:0030145 manganese ion binding
GO:0030976 thiamine pyrophosphate binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0070204 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity
Biological Process
GO:0009234 menaquinone biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2jlc, PDBe:2jlc, PDBj:2jlc
PDBsum2jlc
PubMed18983854
UniProtP17109|MEND_ECOLI 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (Gene Name=menD)

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