Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5WS9

Pyruvate kinase (PYK) from Mycobacterium tuberculosis in complex with Oxalate, ATP and allosteric activator AMP

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006096	biological_process	glycolytic process
A	0016301	molecular_function	kinase activity
A	0030955	molecular_function	potassium ion binding
A	0046872	molecular_function	metal ion 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	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006096	biological_process	glycolytic process
B	0016301	molecular_function	kinase activity
B	0030955	molecular_function	potassium ion binding
B	0046872	molecular_function	metal ion 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	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006096	biological_process	glycolytic process
C	0016301	molecular_function	kinase activity
C	0030955	molecular_function	potassium ion binding
C	0046872	molecular_function	metal ion 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	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006096	biological_process	glycolytic process
D	0016301	molecular_function	kinase activity
D	0030955	molecular_function	potassium ion binding
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 501

Chain	Residue
A	GLU220
A	ASP244
A	OXL502
A	HOH709
A	HOH784

site_id	AC2
Number of Residues	11
Details	binding site for residue OXL A 502

Chain	Residue
A	GLY243
A	ASP244
A	THR276
A	MG501
A	HOH624
A	HOH709
A	HOH784
A	LYS218
A	GLU220
A	ALA241
A	ARG242

site_id	AC3
Number of Residues	20
Details	binding site for residue AMP A 503

Chain	Residue
A	ARG351
A	PHE373
A	THR374
A	GLN375
A	SER376
A	THR379
A	VAL416
A	PRO417
A	LYS418
A	MET419
A	MET425
A	GLY450
A	PRO452
A	PRO453
A	GLY454
A	THR455
A	VAL456
A	GLY457
A	SER458
A	THR459

site_id	AC4
Number of Residues	4
Details	binding site for residue K A 504

Chain	Residue
A	ASN35
A	SER37
A	ASP67
A	SER191

site_id	AC5
Number of Residues	13
Details	binding site for residue ATP A 505

Chain	Residue
A	PRO13
A	ARG33
A	ASN35
A	HIS38
A	SER310
A	GLY311
A	VAL315
A	HOH605
A	HOH630
A	HOH637
A	HOH703
A	HOH786
A	HOH810

site_id	AC6
Number of Residues	8
Details	binding site for residue PO4 A 506

Chain	Residue
A	PRO347
A	ARG348
A	THR349
A	GLY352
A	ARG382
A	ARG385
A	HOH604
A	HOH812

site_id	AC7
Number of Residues	5
Details	binding site for residue MG B 501

Chain	Residue
B	GLU220
B	ASP244
B	OXL502
B	HOH702
B	HOH796

site_id	AC8
Number of Residues	12
Details	binding site for residue OXL B 502

Chain	Residue
B	LYS218
B	GLU220
B	ALA241
B	ARG242
B	GLY243
B	ASP244
B	THR276
B	MG501
B	HOH601
B	HOH630
B	HOH702
B	HOH796

site_id	AC9
Number of Residues	21
Details	binding site for residue AMP B 503

Chain	Residue
B	ARG351
B	PHE373
B	THR374
B	GLN375
B	SER376
B	THR379
B	ALA397
B	VAL416
B	PRO417
B	LYS418
B	MET419
B	MET425
B	GLY450
B	PRO452
B	PRO453
B	GLY454
B	THR455
B	VAL456
B	GLY457
B	SER458
B	THR459

site_id	AD1
Number of Residues	7
Details	binding site for residue K B 504

Chain	Residue
B	ASN35
B	SER37
B	ASP67
B	SER191
B	LYS218
B	HOH689
B	HOH862

site_id	AD2
Number of Residues	13
Details	binding site for residue ATP B 505

Chain	Residue
B	PRO13
B	ARG33
B	ASN35
B	HIS38
B	SER310
B	GLY311
B	VAL315
B	HOH615
B	HOH638
B	HOH645
B	HOH711
B	HOH791
B	HOH862

site_id	AD3
Number of Residues	7
Details	binding site for residue PO4 B 506

Chain	Residue
B	PRO347
B	ARG348
B	THR349
B	GLY352
B	ARG382
B	ARG385
B	HOH603

site_id	AD4
Number of Residues	5
Details	binding site for residue MG C 501

Chain	Residue
C	GLU220
C	ASP244
C	OXL503
C	HOH635
C	HOH680

site_id	AD5
Number of Residues	2
Details	binding site for residue MG C 502

Chain	Residue
C	ATP505
C	HOH649

site_id	AD6
Number of Residues	10
Details	binding site for residue OXL C 503

Chain	Residue
C	LYS218
C	GLU220
C	ALA241
C	ARG242
C	GLY243
C	ASP244
C	THR276
C	MG501
C	HOH635
C	HOH680

site_id	AD7
Number of Residues	21
Details	binding site for residue AMP C 504

Chain	Residue
C	ARG351
C	PHE373
C	THR374
C	GLN375
C	SER376
C	GLY377
C	THR379
C	ALA397
C	VAL416
C	PRO417
C	LYS418
C	MET419
C	MET425
C	GLY450
C	PRO452
C	PRO453
C	GLY454
C	THR455
C	GLY457
C	SER458
C	THR459

site_id	AD8
Number of Residues	17
Details	binding site for residue ATP C 505

Chain	Residue
C	PRO13
C	ARG33
C	ASN35
C	HIS38
C	ARG74
C	ASP125
C	LYS155
C	SER310
C	GLY311
C	VAL315
C	MG502
C	HOH620
C	HOH621
C	HOH631
C	HOH649
C	HOH713
C	HOH827

site_id	AD9
Number of Residues	8
Details	binding site for residue PO4 C 506

Chain	Residue
C	HIS345
C	PRO347
C	ARG348
C	THR349
C	GLY352
C	ARG382
C	ARG385
C	HOH709

site_id	AE1
Number of Residues	5
Details	binding site for residue MG D 501

Chain	Residue
D	GLU220
D	ASP244
D	OXL503
D	HOH638
D	HOH666

site_id	AE2
Number of Residues	4
Details	binding site for residue MG D 502

Chain	Residue
D	ATP506
D	HOH626
D	HOH692
D	HOH857

site_id	AE3
Number of Residues	10
Details	binding site for residue OXL D 503

Chain	Residue
D	LYS218
D	GLU220
D	ALA241
D	ARG242
D	GLY243
D	ASP244
D	THR276
D	MG501
D	HOH637
D	HOH666

site_id	AE4
Number of Residues	20
Details	binding site for residue AMP D 504

Chain	Residue
D	ARG351
D	PHE373
D	THR374
D	GLN375
D	SER376
D	THR379
D	ALA397
D	VAL416
D	PRO417
D	LYS418
D	MET419
D	MET425
D	GLY450
D	PRO452
D	PRO453
D	GLY454
D	THR455
D	GLY457
D	SER458
D	THR459

site_id	AE5
Number of Residues	7
Details	binding site for residue K D 505

Chain	Residue
D	ASN35
D	SER37
D	ASP67
D	SER191
D	LYS218
D	HOH731
D	HOH741

site_id	AE6
Number of Residues	13
Details	binding site for residue ATP D 506

Chain	Residue
D	PRO13
D	ARG33
D	ASN35
D	HIS38
D	ARG74
D	ASP125
D	LYS155
D	SER310
D	GLY311
D	VAL315
D	MG502
D	HOH626
D	HOH731

site_id	AE7
Number of Residues	6
Details	binding site for residue PO4 D 507

Chain	Residue
D	PRO347
D	ARG348
D	THR349
D	GLY352
D	ARG382
D	ARG385

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL213-ILE225

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ARG33
B	ASN35
B	SER37
B	ASP67
B	GLU220
B	GLY243
B	ASP244
B	THR276
C	ARG33
C	ASN35
C	SER37
A	ASN35
C	ASP67
C	GLU220
C	GLY243
C	ASP244
C	THR276
D	ARG33
D	ASN35
D	SER37
D	ASP67
D	GLU220
A	SER37
D	GLY243
D	ASP244
D	THR276
A	ASP67
A	GLU220
A	GLY243
A	ASP244
A	THR276
B	ARG33

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P14618

Chain	Residue	Details
A	ARG74
A	LYS155
B	ARG74
B	LYS155
C	ARG74
C	LYS155
D	ARG74
D	LYS155

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000250

Chain	Residue	Details
A	LYS218
B	LYS218
C	LYS218
D	LYS218

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PknJ; in vitro => ECO:0000269\|PubMed:20520732

Chain	Residue	Details
A	SER37
B	SER37
C	SER37
D	SER37

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