Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6KSH

Crystal structure of pyruvate kinase (PYK) from Plasmodium falciparum in complex with oxalate and ATP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0004743	molecular_function	pyruvate kinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006096	biological_process	glycolytic process
A	0006950	biological_process	response to stress
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0030955	molecular_function	potassium ion binding
A	0046872	molecular_function	metal ion binding
A	0051289	biological_process	protein homotetramerization
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0004743	molecular_function	pyruvate kinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006096	biological_process	glycolytic process
B	0006950	biological_process	response to stress
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0030955	molecular_function	potassium ion binding
B	0046872	molecular_function	metal ion binding
B	0051289	biological_process	protein homotetramerization
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0004743	molecular_function	pyruvate kinase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006096	biological_process	glycolytic process
C	0006950	biological_process	response to stress
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0030955	molecular_function	potassium ion binding
C	0046872	molecular_function	metal ion binding
C	0051289	biological_process	protein homotetramerization
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0004743	molecular_function	pyruvate kinase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006096	biological_process	glycolytic process
D	0006950	biological_process	response to stress
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0030955	molecular_function	potassium ion binding
D	0046872	molecular_function	metal ion binding
D	0051289	biological_process	protein homotetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 601

Chain	Residue
A	GLU257
A	ASP281
A	ATP603
A	OXL605
A	HOH773

site_id	AC2
Number of Residues	4
Details	binding site for residue MG A 602

Chain	Residue
A	ATP603
A	HOH714
A	HOH745
A	HOH794

site_id	AC3
Number of Residues	29
Details	binding site for residue ATP A 603

Chain	Residue
A	THR44
A	LEU45
A	PRO47
A	ARG67
A	ASN69
A	HIS72
A	HIS78
A	ARG109
A	LYS191
A	ASN192
A	LYS255
A	ASP281
A	SER347
A	GLY348
A	ALA351
A	MG601
A	MG602
A	K604
A	OXL605
A	HOH708
A	HOH710
A	HOH714
A	HOH721
A	HOH745
A	HOH763
A	HOH794
A	HOH832
A	HOH839
A	HOH852

site_id	AC4
Number of Residues	7
Details	binding site for residue K A 604

Chain	Residue
A	ASN69
A	SER71
A	ASP102
A	THR103
A	SER228
A	ATP603
A	HOH704

site_id	AC5
Number of Residues	11
Details	binding site for residue OXL A 605

Chain	Residue
A	LYS255
A	GLU257
A	ALA278
A	ARG279
A	GLY280
A	ASP281
A	THR313
A	MG601
A	ATP603
A	HOH714
A	HOH794

site_id	AC6
Number of Residues	5
Details	binding site for residue MG B 601

Chain	Residue
B	GLU257
B	ASP281
B	ATP603
B	OXL605
B	HOH754

site_id	AC7
Number of Residues	5
Details	binding site for residue MG B 602

Chain	Residue
B	SER347
B	ATP603
B	HOH705
B	HOH708
B	HOH743

site_id	AC8
Number of Residues	24
Details	binding site for residue ATP B 603

Chain	Residue
B	THR44
B	LEU45
B	PRO47
B	ARG67
B	ASN69
B	HIS72
B	HIS78
B	ARG109
B	LYS191
B	ASN192
B	LYS255
B	ASP281
B	SER347
B	ALA351
B	MG601
B	MG602
B	K604
B	OXL605
B	HOH705
B	HOH715
B	HOH730
B	HOH735
B	HOH743
B	HOH806

site_id	AC9
Number of Residues	6
Details	binding site for residue K B 604

Chain	Residue
B	ASN69
B	SER71
B	ASP102
B	THR103
B	SER228
B	ATP603

site_id	AD1
Number of Residues	12
Details	binding site for residue OXL B 605

Chain	Residue
B	ARG279
B	GLY280
B	ASP281
B	THR313
B	MG601
B	ATP603
B	HOH705
B	HOH708
B	HOH754
B	LYS255
B	GLU257
B	ALA278

site_id	AD2
Number of Residues	5
Details	binding site for residue MG C 601

Chain	Residue
C	GLU257
C	ASP281
C	ATP603
C	OXL605
C	HOH715

site_id	AD3
Number of Residues	4
Details	binding site for residue MG C 602

Chain	Residue
C	ATP603
C	HOH729
C	HOH731
C	HOH732

site_id	AD4
Number of Residues	23
Details	binding site for residue ATP C 603

Chain	Residue
C	THR44
C	LEU45
C	PRO47
C	ARG67
C	ASN69
C	HIS72
C	ARG109
C	LYS191
C	ASN192
C	LYS255
C	ASP281
C	SER347
C	ALA351
C	MG601
C	MG602
C	K604
C	OXL605
C	HOH702
C	HOH722
C	HOH731
C	HOH732
C	HOH769
C	HOH812

site_id	AD5
Number of Residues	7
Details	binding site for residue K C 604

Chain	Residue
C	ASN69
C	SER71
C	ASP102
C	THR103
C	SER228
C	ATP603
C	HOH707

site_id	AD6
Number of Residues	11
Details	binding site for residue OXL C 605

Chain	Residue
C	LYS255
C	GLU257
C	ALA278
C	ARG279
C	GLY280
C	ASP281
C	THR313
C	MG601
C	ATP603
C	HOH715
C	HOH732

site_id	AD7
Number of Residues	5
Details	binding site for residue MG D 601

Chain	Residue
D	GLU257
D	ASP281
D	ATP603
D	OXL605
D	HOH712

site_id	AD8
Number of Residues	4
Details	binding site for residue MG D 602

Chain	Residue
D	ATP603
D	HOH706
D	HOH742
D	HOH809

site_id	AD9
Number of Residues	28
Details	binding site for residue ATP D 603

Chain	Residue
D	THR44
D	LEU45
D	PRO47
D	ARG67
D	ASN69
D	HIS72
D	HIS78
D	ASP102
D	ARG109
D	LYS191
D	ASN192
D	LYS255
D	ASP281
D	SER347
D	GLY348
D	ALA351
D	MG601
D	MG602
D	K604
D	OXL605
D	HOH706
D	HOH707
D	HOH709
D	HOH742
D	HOH752
D	HOH756
D	HOH809
D	HOH818

site_id	AE1
Number of Residues	7
Details	binding site for residue K D 604

Chain	Residue
D	ASN69
D	SER71
D	ASP102
D	THR103
D	SER228
D	ATP603
D	HOH738

site_id	AE2
Number of Residues	12
Details	binding site for residue OXL D 605

Chain	Residue
D	LYS255
D	GLU257
D	ALA278
D	ARG279
D	GLY280
D	ASP281
D	THR313
D	MG601
D	ATP603
D	HOH712
D	HOH742
D	HOH809

Functional Information from PROSITE/UniProt

site_id	PS00110
Number of Residues	13
Details	PYRUVATE_KINASE Pyruvate kinase active site signature. IkIIPKIENiEGI

Chain	Residue	Details
A	ILE250-ILE262

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)