3HQO

Crystal structures of Leishmania mexicana pyruvate kinase (LmPYK) in complex with ATP and Oxalate

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	0006096	biological_process	glycolytic process
A	0016301	molecular_function	kinase activity
A	0030955	molecular_function	potassium ion binding
A	0032869	biological_process	cellular response to insulin stimulus
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	0006096	biological_process	glycolytic process
B	0016301	molecular_function	kinase activity
B	0030955	molecular_function	potassium ion binding
B	0032869	biological_process	cellular response to insulin stimulus
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	0006096	biological_process	glycolytic process
C	0016301	molecular_function	kinase activity
C	0030955	molecular_function	potassium ion binding
C	0032869	biological_process	cellular response to insulin stimulus
C	0046872	molecular_function	metal ion binding
K	0000287	molecular_function	magnesium ion binding
K	0003824	molecular_function	catalytic activity
K	0004743	molecular_function	pyruvate kinase activity
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0006096	biological_process	glycolytic process
K	0016301	molecular_function	kinase activity
K	0030955	molecular_function	potassium ion binding
K	0032869	biological_process	cellular response to insulin stimulus
K	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG K 500

Chain	Residue
K	ASP145
K	THR296
K	OXL510
K	ATP1001

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG K 502

Chain	Residue
K	LYS238
K	GLU240
K	ASP264
K	OXL510
K	ATP1001

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K K 504

Chain	Residue
K	ASN51
K	SER53
K	ASP83
K	THR84
K	GLU88
K	SER211
K	ATP1001

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OXL K 510

Chain	Residue
K	ARG49
K	LYS238
K	GLU240
K	ALA261
K	GLY263
K	ASP264
K	THR296
K	MG500
K	MG502
K	ATP1001

---

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ATP K 1001

Chain	Residue
K	THR26
K	PRO29
K	ARG49
K	ASN51
K	HIS54
K	TYR59
K	ARG90
K	ASP145
K	ARG175
K	LYS238
K	ASP264
K	SER330
K	LYS335
K	MG500
K	MG502
K	K504
K	OXL510

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 500

Chain	Residue
A	ASP145
A	THR296
A	OXL510
A	ATP1001

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 502

Chain	Residue
A	LYS238
A	GLU240
A	ASP264
A	OXL510
A	ATP1001

---

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K A 504

Chain	Residue
A	ASN51
A	SER53
A	ASP83
A	THR84
A	GLU88
A	SER211
A	ATP1001

---

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OXL A 510

Chain	Residue
A	LYS238
A	GLU240
A	ALA261
A	GLY263
A	ASP264
A	THR296
A	MG500
A	MG502
A	ATP1001

---

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ATP A 1001

Chain	Residue
A	THR26
A	ILE27
A	ARG49
A	ASN51
A	HIS54
A	ARG90
A	ASP145
A	ARG175
A	LYS238
A	ASP264
A	SER330
A	ALA334
A	MG500
A	MG502
A	K504
A	OXL510

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 502

Chain	Residue
B	PHE212
B	GLU240
B	ASP264
B	OXL510

---

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K B 504

Chain	Residue
B	ASN51
B	SER53
B	ASP83
B	THR84
B	GLU88
B	SER211
B	LYS238

---

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OXL B 510

Chain	Residue
B	ASP264
B	THR296
B	MG502
B	ATP1001
B	LYS238
B	GLU240
B	ALA261
B	GLY263

---

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ATP B 1001

Chain	Residue
B	PRO29
B	ARG49
B	ASN51
B	HIS54
B	ARG90
B	ARG175
B	LYS335
B	OXL510

---

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 502

Chain	Residue
C	PHE212
C	GLU240
C	ASP264
C	OXL510

---

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 504

Chain	Residue
C	ASN51
C	SER53
C	ASP83
C	THR84
C	SER211
C	LYS238

---

site_id	BC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OXL C 510

Chain	Residue
C	LYS238
C	GLU240
C	ALA261
C	GLY263
C	ASP264
C	THR296
C	MG502
C	ATP1001

---

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ATP C 1001

Chain	Residue
C	ARG49
C	ASN51
C	HIS54
C	TYR59
C	ARG90
C	ARG175
C	OXL510

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
K	ILE233-VAL245

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
K	ARG49
A	ARG49
A	ASN51
A	SER53
A	ASP83
A	THR84
A	GLU240
A	GLY263
A	ASP264
A	THR296
B	ARG49
K	ASN51
B	ASN51
B	SER53
B	ASP83
B	THR84
B	GLU240
B	GLY263
B	ASP264
B	THR296
C	ARG49
C	ASN51
K	SER53
C	SER53
C	ASP83
C	THR84
C	GLU240
C	GLY263
C	ASP264
C	THR296
K	ASP83
K	THR84
K	GLU240
K	GLY263
K	ASP264
K	THR296

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P14618

Chain	Residue	Details
K	ARG90
A	ARG90
B	ARG90
C	ARG90

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Transition state stabilizer

Chain	Residue	Details
K	LYS238
A	LYS238
B	LYS238
C	LYS238

---