6K0K

Crystal structure of Escherichia coli pyruvate kinase II

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	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006096	biological_process	glycolytic process
A	0016208	molecular_function	AMP binding
A	0016301	molecular_function	kinase activity
A	0030955	molecular_function	potassium ion binding
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	1902912	cellular_component	pyruvate kinase complex
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0004743	molecular_function	pyruvate kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006096	biological_process	glycolytic process
B	0016208	molecular_function	AMP binding
B	0016301	molecular_function	kinase activity
B	0030955	molecular_function	potassium ion binding
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	1902912	cellular_component	pyruvate kinase complex
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0004743	molecular_function	pyruvate kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006096	biological_process	glycolytic process
C	0016208	molecular_function	AMP binding
C	0016301	molecular_function	kinase activity
C	0030955	molecular_function	potassium ion binding
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	1902912	cellular_component	pyruvate kinase complex
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0004743	molecular_function	pyruvate kinase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006096	biological_process	glycolytic process
D	0016208	molecular_function	AMP binding
D	0016301	molecular_function	kinase activity
D	0030955	molecular_function	potassium ion binding
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	1902912	cellular_component	pyruvate kinase complex

Functional Information from PDB Data

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

Chain	Residue
A	GLY189
A	VAL190
A	CYS216
A	ARG412
A	HOH623

---

site_id	AC2
Number of Residues	7
Details	binding site for residue CIT A 502

Chain	Residue
A	LYS448
A	TYR450
A	HOH609
A	GLY62
A	ARG63
A	HIS64
A	PRO425

---

site_id	AC3
Number of Residues	3
Details	binding site for residue MG C 501

Chain	Residue
C	ARG274
C	GLY311
C	ARG397

---

site_id	AC4
Number of Residues	5
Details	binding site for residue MG C 502

Chain	Residue
C	GLU362
C	THR386
C	SER388
C	THR391
C	THR471

---

site_id	AC5
Number of Residues	7
Details	binding site for residue CIT C 503

Chain	Residue
C	GLY62
C	ARG63
C	HIS64
C	PRO425
C	LYS448
C	TYR450
C	HOH607

---

site_id	AC6
Number of Residues	5
Details	binding site for residue MG D 501

Chain	Residue
D	GLU362
D	THR386
D	SER388
D	THR391
D	THR471

---

site_id	AC7
Number of Residues	6
Details	binding site for residue CIT D 502

Chain	Residue
D	GLY62
D	HIS64
D	PRO425
D	LYS448
D	TYR450
D	HOH611

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA218-VAL230

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P30613

Chain	Residue	Details
A	ARG36
B	ARG36
B	ASN38
B	SER40
B	ASP70
B	LYS223
B	GLU225
B	GLY251
B	ASP252
B	THR284
C	ARG36
A	ASN38
C	ASN38
C	SER40
C	ASP70
C	LYS223
C	GLU225
C	GLY251
C	ASP252
C	THR284
D	ARG36
D	ASN38
A	SER40
D	SER40
D	ASP70
D	LYS223
D	GLU225
D	GLY251
D	ASP252
D	THR284
A	ASP70
A	LYS223
A	GLU225
A	GLY251
A	ASP252
A	THR284

---

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

Chain	Residue	Details
A	ARG77
A	LYS160
B	ARG77
B	LYS160
C	ARG77
C	LYS160
D	ARG77
D	LYS160

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549

Chain	Residue	Details
A	LYS223
B	LYS223
C	LYS223
D	LYS223

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842

Chain	Residue	Details
A	LYS351
B	LYS351
C	LYS351
D	LYS351

---