Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6NN5

The structure of human liver pyruvate kinase, hLPYK-W527H

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0001666	biological_process	response to hypoxia
A	0003824	molecular_function	catalytic activity
A	0004743	molecular_function	pyruvate kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006096	biological_process	glycolytic process
A	0007584	biological_process	response to nutrient
A	0009749	biological_process	response to glucose
A	0010038	biological_process	response to metal ion
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0030955	molecular_function	potassium ion binding
A	0032869	biological_process	cellular response to insulin stimulus
A	0033198	biological_process	response to ATP
A	0042866	biological_process	pyruvate biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0048029	molecular_function	monosaccharide binding
A	0051591	biological_process	response to cAMP
A	0070062	cellular_component	extracellular exosome
A	0071872	biological_process	cellular response to epinephrine stimulus
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0001666	biological_process	response to hypoxia
B	0003824	molecular_function	catalytic activity
B	0004743	molecular_function	pyruvate kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006096	biological_process	glycolytic process
B	0007584	biological_process	response to nutrient
B	0009749	biological_process	response to glucose
B	0010038	biological_process	response to metal ion
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0030955	molecular_function	potassium ion binding
B	0032869	biological_process	cellular response to insulin stimulus
B	0033198	biological_process	response to ATP
B	0042866	biological_process	pyruvate biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0048029	molecular_function	monosaccharide binding
B	0051591	biological_process	response to cAMP
B	0070062	cellular_component	extracellular exosome
B	0071872	biological_process	cellular response to epinephrine stimulus
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0001666	biological_process	response to hypoxia
C	0003824	molecular_function	catalytic activity
C	0004743	molecular_function	pyruvate kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006096	biological_process	glycolytic process
C	0007584	biological_process	response to nutrient
C	0009749	biological_process	response to glucose
C	0010038	biological_process	response to metal ion
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0030955	molecular_function	potassium ion binding
C	0032869	biological_process	cellular response to insulin stimulus
C	0033198	biological_process	response to ATP
C	0042866	biological_process	pyruvate biosynthetic process
C	0046872	molecular_function	metal ion binding
C	0048029	molecular_function	monosaccharide binding
C	0051591	biological_process	response to cAMP
C	0070062	cellular_component	extracellular exosome
C	0071872	biological_process	cellular response to epinephrine stimulus
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0001666	biological_process	response to hypoxia
D	0003824	molecular_function	catalytic activity
D	0004743	molecular_function	pyruvate kinase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006096	biological_process	glycolytic process
D	0007584	biological_process	response to nutrient
D	0009749	biological_process	response to glucose
D	0010038	biological_process	response to metal ion
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0030955	molecular_function	potassium ion binding
D	0032869	biological_process	cellular response to insulin stimulus
D	0033198	biological_process	response to ATP
D	0042866	biological_process	pyruvate biosynthetic process
D	0046872	molecular_function	metal ion binding
D	0048029	molecular_function	monosaccharide binding
D	0051591	biological_process	response to cAMP
D	0070062	cellular_component	extracellular exosome
D	0071872	biological_process	cellular response to epinephrine stimulus

Functional Information from PDB Data

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

Chain	Residue
A	THR444
A	THR445
A	THR446
A	SER449
A	GLY532

site_id	AC2
Number of Residues	8
Details	binding site for residue GOL A 602

Chain	Residue
A	ARG306
A	GLY307
A	ASP308
A	THR340
A	ARG85
A	LYS282
A	GLU284
A	ALA305

site_id	AC3
Number of Residues	4
Details	binding site for residue GOL A 603

Chain	Residue
A	HIS403
A	ARG404
A	ARG459
C	ARG411

site_id	AC4
Number of Residues	6
Details	binding site for residue GOL A 604

Chain	Residue
A	HIS527
A	ARG528
A	ASN535
C	ARG538
C	VAL539
C	LEU540

site_id	AC5
Number of Residues	2
Details	binding site for residue EDO A 605

Chain	Residue
A	ASP293
A	GLU297

site_id	AC6
Number of Residues	3
Details	binding site for residue EDO A 606

Chain	Residue
A	LYS278
A	GLN451
A	VAL475

site_id	AC7
Number of Residues	4
Details	binding site for residue EDO A 607

Chain	Residue
A	LYS323
A	ASP366
A	HOH723
D	HOH730

site_id	AC8
Number of Residues	5
Details	binding site for residue GOL B 601

Chain	Residue
B	THR444
B	THR445
B	THR446
B	SER449
B	GLY532

site_id	AC9
Number of Residues	8
Details	binding site for residue GOL B 602

Chain	Residue
B	ARG85
B	LYS282
B	GLU284
B	ALA305
B	ARG306
B	GLY307
B	ASP308
B	THR340

site_id	AD1
Number of Residues	9
Details	binding site for residue EDO B 603

Chain	Residue
B	GLY333
B	LYS334
B	PRO335
B	ASP369
B	GLN451
B	SER454
B	ARG455
B	ARG457
B	CYS478

site_id	AD2
Number of Residues	3
Details	binding site for residue EDO B 604

Chain	Residue
B	ARG267
B	VAL298
B	ASP300

site_id	AD3
Number of Residues	3
Details	binding site for residue GOL C 601

Chain	Residue
C	GLU94
D	HIS93
D	GLU94

site_id	AD4
Number of Residues	6
Details	binding site for residue GOL C 602

Chain	Residue
C	THR444
C	THR445
C	THR446
C	ARG448
C	SER449
C	GLY532

site_id	AD5
Number of Residues	7
Details	binding site for residue GOL C 603

Chain	Residue
C	ARG85
C	LYS282
C	ALA305
C	ARG306
C	GLY307
C	ASP308
C	THR340

site_id	AD6
Number of Residues	6
Details	binding site for residue EDO C 604

Chain	Residue
C	ALA97
C	ILE100
C	ALA101
C	HIS247
D	GLU94
D	GLU98

site_id	AD7
Number of Residues	5
Details	binding site for residue EDO C 605

Chain	Residue
B	LEU42
C	ASN330
C	ASP366
C	LEU406
C	HOH725

site_id	AD8
Number of Residues	5
Details	binding site for residue EDO C 606

Chain	Residue
C	LYS278
C	THR446
C	GLY447
C	GLN451
C	GLN474

site_id	AD9
Number of Residues	3
Details	binding site for residue GOL D 601

Chain	Residue
D	ARG55
D	HIS391
D	HOH747

site_id	AE1
Number of Residues	8
Details	binding site for residue GOL D 602

Chain	Residue
D	THR340
D	ARG85
D	LYS282
D	GLU284
D	ALA305
D	ARG306
D	GLY307
D	ASP308

site_id	AE2
Number of Residues	5
Details	binding site for residue GOL D 603

Chain	Residue
D	THR444
D	THR445
D	THR446
D	SER449
D	GLY532

site_id	AE3
Number of Residues	3
Details	binding site for residue EDO D 604

Chain	Residue
D	TRP494
D	ARG501
D	PRO529

site_id	AE4
Number of Residues	5
Details	binding site for residue EDO D 605

Chain	Residue
D	ASN381
D	PHE382
D	PRO383
D	VAL384
D	GLU385

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE277-VAL289

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11960989","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VGB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	13
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	80
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11960989","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VGF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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