5SCH

Structure of liver pyruvate kinase in complex with anthraquinone derivative 100

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	0006096	biological_process	glycolytic process
A	0030955	molecular_function	potassium ion binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0004743	molecular_function	pyruvate kinase activity
B	0006096	biological_process	glycolytic process
B	0030955	molecular_function	potassium ion binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0004743	molecular_function	pyruvate kinase activity
C	0006096	biological_process	glycolytic process
C	0030955	molecular_function	potassium ion binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0004743	molecular_function	pyruvate kinase activity
D	0006096	biological_process	glycolytic process
D	0030955	molecular_function	potassium ion binding
E	0000287	molecular_function	magnesium ion binding
E	0003824	molecular_function	catalytic activity
E	0004743	molecular_function	pyruvate kinase activity
E	0006096	biological_process	glycolytic process
E	0030955	molecular_function	potassium ion binding
F	0000287	molecular_function	magnesium ion binding
F	0003824	molecular_function	catalytic activity
F	0004743	molecular_function	pyruvate kinase activity
F	0006096	biological_process	glycolytic process
F	0030955	molecular_function	potassium ion binding
G	0000287	molecular_function	magnesium ion binding
G	0003824	molecular_function	catalytic activity
G	0004743	molecular_function	pyruvate kinase activity
G	0006096	biological_process	glycolytic process
G	0030955	molecular_function	potassium ion binding
H	0000287	molecular_function	magnesium ion binding
H	0003824	molecular_function	catalytic activity
H	0004743	molecular_function	pyruvate kinase activity
H	0006096	biological_process	glycolytic process
H	0030955	molecular_function	potassium ion binding

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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB

Chain	Residue	Details
A	ARG85
E	SER89
F	ARG85
F	SER89
G	ARG85
G	SER89
H	ARG85
H	SER89
A	SER89
B	ARG85
B	SER89
C	ARG85
C	SER89
D	ARG85
D	SER89
E	ARG85

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site_id	SWS_FT_FI2
Number of Residues	96
Details	BINDING: BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF

Chain	Residue	Details
A	ASN87
A	TRP494
A	ARG501
A	ARG528
B	ASN87
B	ASP125
B	THR126
B	LYS282
B	GLU284
B	GLY307
B	ASP308
A	ASP125
B	THR340
B	THR444
B	TRP494
B	ARG501
B	ARG528
C	ASN87
C	ASP125
C	THR126
C	LYS282
C	GLU284
A	THR126
C	GLY307
C	ASP308
C	THR340
C	THR444
C	TRP494
C	ARG501
C	ARG528
D	ASN87
D	ASP125
D	THR126
A	LYS282
D	LYS282
D	GLU284
D	GLY307
D	ASP308
D	THR340
D	THR444
D	TRP494
D	ARG501
D	ARG528
E	ASN87
A	GLU284
E	ASP125
E	THR126
E	LYS282
E	GLU284
E	GLY307
E	ASP308
E	THR340
E	THR444
E	TRP494
E	ARG501
A	GLY307
E	ARG528
F	ASN87
F	ASP125
F	THR126
F	LYS282
F	GLU284
F	GLY307
F	ASP308
F	THR340
F	THR444
A	ASP308
F	TRP494
F	ARG501
F	ARG528
G	ASN87
G	ASP125
G	THR126
G	LYS282
G	GLU284
G	GLY307
G	ASP308
A	THR340
G	THR340
G	THR444
G	TRP494
G	ARG501
G	ARG528
H	ASN87
H	ASP125
H	THR126
H	LYS282
H	GLU284
A	THR444
H	GLY307
H	ASP308
H	THR340
H	THR444
H	TRP494
H	ARG501
H	ARG528

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site_id	SWS_FT_FI3
Number of Residues	8
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549

Chain	Residue	Details
A	LYS282
B	LYS282
C	LYS282
D	LYS282
E	LYS282
F	LYS282
G	LYS282
H	LYS282

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site_id	SWS_FT_FI4
Number of Residues	16
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	ASP12
E	SER261
F	ASP12
F	SER261
G	ASP12
G	SER261
H	ASP12
H	SER261
A	SER261
B	ASP12
B	SER261
C	ASP12
C	SER261
D	ASP12
D	SER261
E	ASP12

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