Structure of PDB 1w6t Chain A

Receptor sequence
>1w6tA (length=428) Species: 170187 (Streptococcus pneumoniae TIGR4) [Search protein sequence]
HMSIITDVYAREVLDSRGNPTLEVEVYTESGAFGRGMVPSGGEHEAVELR
DGDKSRYGGLGTQKAVDNVNNIIAEAIIGYDVRDQQAIDRAMIALDGTPN
KGKLGANAILGVSIAVARAAADYLEIPLYSYLGGFNTKVLPTPMMNIING
GSHSDAPIAFQEFMILPVGAPTFKEALRYGAEIFHALKKILKSRGLETAV
GDEGGFAPRFEGTEDGVETILAAIEAAGYVPGKDVFLGFDCASSEFYDRK
VYDYTKFEGEGAAVRTSAEQIDYLEELVNKYPIITIEDGMDENDWDGWKA
LTERLGKKVQLVGDDFFVTNTDYLARGIQEGAANSILIKVNQIGTLTETF
EAIEMAKEAGYTAVVSHRSGETEDSTIADIAVATNAGQIKTGSLSRTDRI
AKYNQLLRIEDQLGEVAEYRGLKSFYNL
3D structure
PDB1w6t Plasmin(Ogen)-Binding Alpha-Enolase from Streptococcus Pneumoniae: Crystal Structure and Evaluation of Plasmin(Ogen)-Binding Sites
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H155 E164 E205 D242 E291 D318 K343 H371 K394
Catalytic site (residue number reindexed from 1) H153 E162 E203 D240 E287 D314 K339 H367 K390
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 MG A D242 E291 D318 D240 E287 D314
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004634 phosphopyruvate hydratase activity
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006096 glycolytic process
GO:0007155 cell adhesion
Cellular Component
GO:0000015 phosphopyruvate hydratase complex
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0009274 peptidoglycan-based cell wall
GO:0009986 cell surface
GO:0042603 capsule

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1w6t, PDBe:1w6t, PDBj:1w6t
PDBsum1w6t
PubMed15476816
UniProtQ97QS2|ENO_STRPN Enolase (Gene Name=eno)

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