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Structure of PDB 6d3q Chain C

Receptor sequence >6d3qC (length=437) Species: 562 (Escherichia coli) [Search protein sequence] QQMGRGSMSKIVKIIGREIIDSRGNPTVEAEVHLEGGFVGMAAAPSGAST GSREALELRDGDKSRFLGKGVTKAVAAVNGPIAQALIGKDAKDQAGIDKI MIDLDGTENKSKFGANAILAVSLANAKAAAAAKGMPLYEHIAELNGTPGK YSMPVPMMNIINGGEHADNNVDIQEFMIQPVGAKTVKEAIRMGSEVFHHL AKVLKAKGMNTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKDITL AMDCAASEFYKDGKYVLAGEGNFTSEEFTHFLEELTKQYPIVSIEDGLDE SDWDGFAYQTKVLGDKIQLVGDDLFVTNTKILKEGIEKGIANSILIKFNQ IGSLTETLAAIKMAKDAGYTAVISHRSGETEDATIADLAVGTAAGQIKTG SMSRSDRVAKYNQLIRIEEALGEKAPYNGRKEIKGQA

3D structure PDB 6d3q Functional and structural basis of E. coli enolase inhibition by SF2312: a mimic of the carbanion intermediate. Chain C Resolution 2.24 Å 3D structure Catalytic site residues are labeled in the structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

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) S49 H166 E175 E216 D253 E295 D322 K347 H375 K398 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 4NG C G39 S41 E167 E208 D245 E289 D316 K341 R370 S371 K392 G47 S49 E175 E216 D253 E295 D322 K347 R376 S377 K398 MOAD: Ki=3.4nM BS02 MG C D245 E289 D316 D253 E295 D322

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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