3QV7

Crystal structure of Leishmania mexicana pyruvate kinase(LmPYK)in complex with ponceau S and acid blue 25.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0006096	biological_process	glycolytic process
A	0006950	biological_process	response to stress
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0030955	molecular_function	potassium ion binding
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide 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	0006096	biological_process	glycolytic process
B	0006950	biological_process	response to stress
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0030955	molecular_function	potassium ion binding
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide 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	0006096	biological_process	glycolytic process
C	0006950	biological_process	response to stress
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0030955	molecular_function	potassium ion binding
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide 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	0006096	biological_process	glycolytic process
D	0006950	biological_process	response to stress
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase 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	6
Details	BINDING SITE FOR RESIDUE SO4 D 499

Chain	Residue
D	PRO87
D	GLU88
D	ILE89
D	VAL177
D	ASN178
D	PHE212

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 500

Chain	Residue
D	ARG404
D	SER405
D	ALA481
D	ASP482
D	SER400
D	ASN401
D	THR402

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K D 501

Chain	Residue
D	ASN51
D	SER53
D	THR84
D	LYS238

---

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE K D 502

Chain	Residue
D	ASP264

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE QV7 D 503

Chain	Residue
D	HIS54
D	GLY55
D	GLY55
D	SER56
D	SER56
D	TYR59
D	TYR59
D	LYS335

---

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE QV7 A 499

Chain	Residue
A	SER53
A	HIS54
A	GLY55
A	LYS335
A	HOH655
B	ARG231
B	ARG404
B	ARG407
B	QV7499
B	QV8500

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 500

Chain	Residue
A	SER400
A	ASN401
A	THR402
A	GLY403
A	ARG404
A	SER405

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE K A 501

Chain	Residue
A	GLU240
A	ASP264

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K A 502

Chain	Residue
A	GLN354
A	LEU357
A	GLU359

---

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE QV7 B 499

Chain	Residue
A	THR26
A	PRO29
A	ASN51
A	HIS54
A	GLY55
A	SER56
A	TYR59
A	ALA334
A	LYS335
A	QV7499
B	THR402
B	ARG404
B	ASP482
B	HIS483
B	LYS486
B	HOH514

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE QV8 B 500

Chain	Residue
A	QV7499
B	ARG231
B	ASP232
B	THR402
B	ARG424

---

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE QV7 B 501

Chain	Residue
A	SER1
B	SER1
B	TYR360
B	VAL361
B	ASN364
B	QV7504
D	ASN364
D	LYS368
D	HOH507

---

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K B 503

Chain	Residue
B	GLN354
B	LEU357
B	GLU359
B	HOH575

---

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE QV7 B 504

Chain	Residue
A	SER1
A	TYR360
A	VAL361
A	ASN364
B	SER1
B	QV7501
C	SER1
C	VAL361
C	LYS368

---

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 499

Chain	Residue
C	SER400
C	ASN401
C	THR402
C	ARG404
C	SER405
C	ALA481
C	ASP482

---

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 500

Chain	Residue
C	ASP83
C	THR84
C	LYS238
C	HOH656
C	ASN51
C	SER53

---

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K C 501

Chain	Residue
C	GLN354
C	LEU357
C	GLU359

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
D	ILE233-VAL245

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

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