Structure of PDB 4rop Chain A

Receptor sequence
>4ropA (length=424) Species: 1140 (Synechococcus elongatus PCC 7942 = FACHB-805) [Search protein sequence]
YGTQIAEITAREILDSRGRPTVEAEVHLEDGSVGLAQVPSGASTGTFEAH
ELRDDDPSRYGGKGVQKAVENVSAIEDALIGLSALDQEGLDKAMIALDGT
PNKKNLGANAILAVSLATAHAAATSLNLPLYRYLGGPLANVLPVPMMNVI
NGGAHADNNVDFQEFMIMPVGAPSFKEALRWGAEVFHALAKVLKDKGLAT
GVGDEGGFAPNLGSNKEALELLLTAIEAAGYKPGEQVALAMDVASSEFYK
NGLYTCDGVSHEPAGMIGILADLVSQYPIVSIEDGLQEDDWSNWKTLTQQ
LGSTVQLVGDDLFVTNPDRLQSGIEQGVGNAVLIKLNQIGTLTETLRTID
LATRSGYRSVISHRSGETEDTTIADLAVATRAGQIKTGSLSRSERIAKYN
RLLRIEAALGENALYAGAIGLGPK
3D structure
PDB4rop The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding
ChainA
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S47 H159 E168 E209 D246 E287 D314 K339 H367 K390
Catalytic site (residue number reindexed from 1) S43 H155 E164 E205 D242 E283 D310 K335 H363 K386
Enzyme Commision number 4.2.1.11: phosphopyruvate hydratase.
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 CA A D246 E287 D314 D242 E283 D310
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004634 phosphopyruvate hydratase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006096 glycolytic process
Cellular Component
GO:0000015 phosphopyruvate hydratase complex
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0009986 cell surface

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Molecular Function
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Cellular Component
External links
PDB RCSB:4rop, PDBe:4rop, PDBj:4rop
PDBsum4rop
PubMed
UniProtQ31QJ8|ENO_SYNE7 Enolase (Gene Name=eno)

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