1E0U

Structure R271L mutant of E. coli pyruvate kinase

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	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	0006950	biological_process	response to stress
A	0009408	biological_process	response to heat
A	0016020	cellular_component	membrane
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase 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	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	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	0006950	biological_process	response to stress
B	0009408	biological_process	response to heat
B	0016020	cellular_component	membrane
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase 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	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	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	0006950	biological_process	response to stress
C	0009408	biological_process	response to heat
C	0016020	cellular_component	membrane
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase 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	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	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	0006950	biological_process	response to stress
D	0009408	biological_process	response to heat
D	0016020	cellular_component	membrane
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase 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	7
Details	BINDING SITE FOR RESIDUE SO4 A 701

Chain	Residue
A	THR378
A	GLN379
A	GLY380
A	GLY381
A	LYS382
A	SER383
A	GLY460

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 702

Chain	Residue
B	GLY380
B	GLY381
B	LYS382
B	SER383
B	GLY460
B	HOH2055
B	THR378
B	GLN379

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 C 703

Chain	Residue
C	THR378
C	GLN379
C	GLY380
C	GLY381
C	LYS382
C	SER383
C	SER459
C	GLY460

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 D 704

Chain	Residue
D	THR378
D	GLN379
D	GLY380
D	GLY381
D	LYS382
D	SER383
D	GLY460
D	HOH2058
D	HOH2059

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE215-LEU227

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P30613","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	20
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","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1pkn

Chain	Residue	Details
A	THR278
A	GLU314
A	LYS220
A	ARG32
A	ARG73
A	SER312

---

site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1pkn

Chain	Residue	Details
B	THR278
B	GLU314
B	LYS220
B	ARG32
B	ARG73
B	SER312

---

site_id	CSA3
Number of Residues	6
Details	Annotated By Reference To The Literature 1pkn

Chain	Residue	Details
C	THR278
C	GLU314
C	LYS220
C	ARG32
C	ARG73
C	SER312

---

site_id	CSA4
Number of Residues	6
Details	Annotated By Reference To The Literature 1pkn

Chain	Residue	Details
D	THR278
D	GLU314
D	LYS220
D	ARG32
D	ARG73
D	SER312

---