Structure of PDB 2fym Chain D Binding Site BS01
Receptor Information
>2fym Chain D (length=427) Species:
562
(Escherichia coli) [
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SKIVKIIGREIIDSRGNPTVEAEVHLEGGFVGMAAAPSGASTGSREALEL
RDGDKSRFLGKGVTKAVAAVNGPIAQALIGKDAKDQAGIDKIMIDLDGTE
NKSKFGANAILAVSLANAKAAAAAKGMPLYEHIAELNGTPGKYSMPVPMM
NIINGGEHADNNVDIQEFMIQPVGAKTVKEAIRMGSEVFHHLAKVLKAKG
MNTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKDITLAMDCAASE
FYKDGKYVLANKAFTSEEFTHFLEELTKQYPIVSIEDGLDESDWDGFAYQ
TKVLGDKIQLVGDDLFVTNTKILKEGIEKGIANSILIKFNQIGSLTETLA
AIKMAKDAGYTAVISHRSGETEDATIADLAVGTAAGQIKTGSMSRSDRVA
KYNQLIRIEEALGEKAPYNGRKEIKGQ
Ligand information
>2fym Chain E (length=15) Species:
83333
(Escherichia coli K-12) [
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ASPELASGKVWIRYP
Receptor-Ligand Complex Structure
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PDB
2fym
Recognition of Enolase in the Escherichia coli RNA Degradosome
Resolution
1.6 Å
Binding residue
(original residue number in PDB)
V4 K5 I7 H25 G28 G29 M33 K119 Q407
Binding residue
(residue number reindexed from 1)
V4 K5 I7 H25 G28 G29 M33 K119 Q404
Enzymatic activity
Catalytic site (original residue number in PDB)
S41 H158 E167 E208 D245 E289 D316 K341 H369 K392
Catalytic site (residue number reindexed from 1)
S41 H158 E167 E208 D245 E286 D313 K338 H366 K389
Enzyme Commision number
4.2.1.11
: phosphopyruvate hydratase.
Gene Ontology
Molecular Function
GO:0000287
magnesium ion binding
GO:0004634
phosphopyruvate hydratase activity
GO:0005515
protein binding
GO:0016829
lyase activity
GO:0042802
identical protein binding
GO:0042803
protein homodimerization activity
GO:0046872
metal ion binding
Biological Process
GO:0006096
glycolytic process
GO:0006396
RNA processing
GO:0006401
RNA catabolic process
Cellular Component
GO:0000015
phosphopyruvate hydratase complex
GO:0005576
extracellular region
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0005856
cytoskeleton
GO:0009986
cell surface
GO:0016020
membrane
GO:1990061
bacterial degradosome
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:2fym
,
PDBe:2fym
,
PDBj:2fym
PDBsum
2fym
PubMed
16516921
UniProt
P0A6P9
|ENO_ECOLI Enolase (Gene Name=eno)
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