7QZU

Structure of liver pyruvate kinase in complex with anthraquinone derivative 47

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
A	SER89
B	ARG85
B	SER89
C	ARG85
C	SER89
D	ARG85
D	SER89
E	ARG85
E	SER89
F	ARG85
F	SER89
G	ARG85
G	SER89
H	ARG85
H	SER89

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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	ASP125
A	THR126
A	GLY380
A	PHE382
A	GLN405
A	LEU406
A	ALA438
A	ILE542
B	ASN87
B	ASP125
B	THR126
B	GLY380
B	PHE382
B	GLN405
B	LEU406
B	ALA438
B	ILE542
C	ASN87
C	ASP125
C	THR126
C	GLY380
C	PHE382
C	GLN405
C	LEU406
C	ALA438
C	ILE542
D	ASN87
D	ASP125
D	THR126
D	GLY380
D	PHE382
D	GLN405
D	LEU406
D	ALA438
D	ILE542
E	ASN87
E	ASP125
E	THR126
E	GLY380
E	PHE382
E	GLN405
E	LEU406
E	ALA438
E	ILE542
F	ASN87
F	ASP125
F	THR126
F	GLY380
F	PHE382
F	GLN405
F	LEU406
F	ALA438
F	ILE542
G	ASN87
G	ASP125
G	THR126
G	GLY380
G	PHE382
G	GLN405
G	LEU406
G	ALA438
G	ILE542
H	ASN87
H	ASP125
H	THR126
H	GLY380
H	PHE382
H	GLN405
H	LEU406
H	ALA438
H	ILE542

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site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P14618

Chain	Residue	Details
A	GLY132
A	LYS317
B	GLY230
B	LYS317
C	GLY132
C	LYS317
D	GLY132
D	LYS317
E	GLY132
E	LYS317
F	GLY132
F	LYS317
G	GLY132
G	LYS317
H	GLY132
H	LYS317

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549

Chain	Residue	Details
A	GLY380
B	GLY380
C	GLY380
D	GLY380
E	GLY380
F	GLY380
G	GLY380
H	GLY380

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site_id	SWS_FT_FI5
Number of Residues	16
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	ASP12
A	ASP359
B	ASP12
B	ASP359
C	ASP12
C	ASP359
D	ASP12
D	ASP359
E	ASP12
E	ASP359
F	ASP12
F	ASP359
G	ASP12
G	ASP359
H	ASP12
H	ASP359

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