Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6WP6

Pyruvate Kinase M2 mutant-S37E K433E

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003723	molecular_function	RNA binding
A	0003729	molecular_function	mRNA binding
A	0003824	molecular_function	catalytic activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0004743	molecular_function	pyruvate kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005576	cellular_component	extracellular region
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005791	cellular_component	rough endoplasmic reticulum
A	0005829	cellular_component	cytosol
A	0005929	cellular_component	cilium
A	0006096	biological_process	glycolytic process
A	0006417	biological_process	regulation of translation
A	0012501	biological_process	programmed cell death
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0023026	molecular_function	MHC class II protein complex binding
A	0030955	molecular_function	potassium ion binding
A	0031982	cellular_component	vesicle
A	0032869	biological_process	cellular response to insulin stimulus
A	0034774	cellular_component	secretory granule lumen
A	0045296	molecular_function	cadherin binding
A	0046872	molecular_function	metal ion binding
A	0061621	biological_process	canonical glycolysis
A	0062023	cellular_component	collagen-containing extracellular matrix
A	0070062	cellular_component	extracellular exosome
A	1903561	cellular_component	extracellular vesicle
A	1903672	biological_process	positive regulation of sprouting angiogenesis
A	1904813	cellular_component	ficolin-1-rich granule lumen
A	2000767	biological_process	positive regulation of cytoplasmic translation
C	0000287	molecular_function	magnesium ion binding
C	0003723	molecular_function	RNA binding
C	0003729	molecular_function	mRNA binding
C	0003824	molecular_function	catalytic activity
C	0004713	molecular_function	protein tyrosine kinase activity
C	0004743	molecular_function	pyruvate kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005576	cellular_component	extracellular region
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005791	cellular_component	rough endoplasmic reticulum
C	0005829	cellular_component	cytosol
C	0005929	cellular_component	cilium
C	0006096	biological_process	glycolytic process
C	0006417	biological_process	regulation of translation
C	0012501	biological_process	programmed cell death
C	0016301	molecular_function	kinase activity
C	0016310	biological_process	phosphorylation
C	0023026	molecular_function	MHC class II protein complex binding
C	0030955	molecular_function	potassium ion binding
C	0031982	cellular_component	vesicle
C	0032869	biological_process	cellular response to insulin stimulus
C	0034774	cellular_component	secretory granule lumen
C	0045296	molecular_function	cadherin binding
C	0046872	molecular_function	metal ion binding
C	0061621	biological_process	canonical glycolysis
C	0062023	cellular_component	collagen-containing extracellular matrix
C	0070062	cellular_component	extracellular exosome
C	1903561	cellular_component	extracellular vesicle
C	1903672	biological_process	positive regulation of sprouting angiogenesis
C	1904813	cellular_component	ficolin-1-rich granule lumen
C	2000767	biological_process	positive regulation of cytoplasmic translation

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	ILE265-VAL277

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:23064226

Chain	Residue	Details
C	ASN70
C	ARG106
C	HIS464
A	ASN70
A	ARG106
A	HIS464

site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P30613

Chain	Residue	Details
C	ARG73
A	THR328
C	LYS270
C	GLY295
C	ASP296
C	THR328
A	ARG73
A	LYS270
A	GLY295
A	ASP296

site_id	SWS_FT_FI3
Number of Residues	14
Details	BINDING: BINDING => ECO:0000269\|PubMed:23530218, ECO:0007744\|PDB:4FXF

Chain	Residue	Details
C	ASN75
A	ASP113
A	THR114
A	ARG120
A	LYS207
A	GLU272
C	SER77
C	ASP113
C	THR114
C	ARG120
C	LYS207
C	GLU272
A	ASN75
A	SER77

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:15996096, ECO:0000269\|PubMed:23530218, ECO:0007744\|PDB:1T5A, ECO:0007744\|PDB:4FXF

Chain	Residue	Details
C	THR432
C	TRP482
C	ARG489
C	ARG516
A	THR432
A	TRP482
A	ARG489
A	ARG516

site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000250\|UniProtKB:P00549

Chain	Residue	Details
C	LYS270
A	LYS270

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Crucial for phosphotyrosine binding => ECO:0000269\|PubMed:27199445

Chain	Residue	Details
C	GLU433
A	GLU433

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0000269\|Ref.11, ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:25944712

Chain	Residue	Details
C	SER2
A	SER2

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N6,N6,N6-trimethyllysine => ECO:0007744\|PubMed:24129315

Chain	Residue	Details
C	LYS3
A	LYS3

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:16964243, ECO:0007744\|PubMed:17081983, ECO:0007744\|PubMed:18088087, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:18691976, ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
C	GLU37
A	GLU37

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
C	THR41
A	THR41

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
C	LYS62
C	LYS89
A	LYS62
A	LYS89

site_id	SWS_FT_FI12
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P52480

Chain	Residue	Details
C	LYS66
C	LYS498
A	LYS66
A	LYS498

site_id	SWS_FT_FI13
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P11980

Chain	Residue	Details
C	SER97
C	SER100
A	SER97
A	SER100

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:15592455, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
C	TYR105
A	TYR105

site_id	SWS_FT_FI15
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
C	SER127
A	SER127

site_id	SWS_FT_FI16
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P52480

Chain	Residue	Details
C	TYR148
A	TYR148

site_id	SWS_FT_FI17
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P52480

Chain	Residue	Details
C	LYS166
C	LYS322
A	LYS166
A	LYS322

site_id	SWS_FT_FI18
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:19690332

Chain	Residue	Details
C	TYR175
A	TYR175

site_id	SWS_FT_FI19
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:19690332

Chain	Residue	Details
C	THR195
A	THR195

site_id	SWS_FT_FI20
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
C	LYS266
A	LYS266

site_id	SWS_FT_FI21
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250\|UniProtKB:P52480

Chain	Residue	Details
C	LYS270
A	LYS270

site_id	SWS_FT_FI22
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:21700219

Chain	Residue	Details
C	LYS305
A	LYS305

site_id	SWS_FT_FI23
Number of Residues	4
Details	MOD_RES: 4-hydroxyproline => ECO:0000269\|PubMed:21620138

Chain	Residue	Details
C	PRO403
C	PRO408
A	PRO403
A	PRO408

site_id	SWS_FT_FI24
Number of Residues	4
Details	MOD_RES: S-nitrosocysteine => ECO:0000269\|PubMed:30487609

Chain	Residue	Details
C	CYS423
C	CYS424
A	CYS423
A	CYS424

site_id	SWS_FT_FI25
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:24120661, ECO:0000269\|PubMed:26787900, ECO:0007744\|PubMed:19608861

Chain	Residue	Details
C	GLU433
A	GLU433

site_id	SWS_FT_FI26
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P52480

Chain	Residue	Details
C	LYS475
A	LYS475

site_id	SWS_FT_FI27
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
C	LYS115
A	LYS115

site_id	SWS_FT_FI28
Number of Residues	6
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
C	LYS266
C	LYS270
A	LYS266
A	LYS270

site_id	SWS_FT_FI29
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744\|PubMed:25114211

Chain	Residue	Details
C	LYS166
A	LYS166

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