4I7E

Crystal Structure of the Bacillus stearothermophilus Phosphofructokinase Mutant D12A in Complex with PEP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003872	molecular_function	6-phosphofructokinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005945	cellular_component	6-phosphofructokinase complex
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006096	biological_process	glycolytic process
A	0008443	molecular_function	phosphofructokinase activity
A	0016020	cellular_component	membrane
A	0016208	molecular_function	AMP binding
A	0016301	molecular_function	kinase activity
A	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0048029	molecular_function	monosaccharide binding
A	0061621	biological_process	canonical glycolysis
A	0070095	molecular_function	fructose-6-phosphate binding
B	0003872	molecular_function	6-phosphofructokinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005945	cellular_component	6-phosphofructokinase complex
B	0006002	biological_process	fructose 6-phosphate metabolic process
B	0006096	biological_process	glycolytic process
B	0008443	molecular_function	phosphofructokinase activity
B	0016020	cellular_component	membrane
B	0016208	molecular_function	AMP binding
B	0016301	molecular_function	kinase activity
B	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0048029	molecular_function	monosaccharide binding
B	0061621	biological_process	canonical glycolysis
B	0070095	molecular_function	fructose-6-phosphate binding
C	0003872	molecular_function	6-phosphofructokinase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005945	cellular_component	6-phosphofructokinase complex
C	0006002	biological_process	fructose 6-phosphate metabolic process
C	0006096	biological_process	glycolytic process
C	0008443	molecular_function	phosphofructokinase activity
C	0016020	cellular_component	membrane
C	0016208	molecular_function	AMP binding
C	0016301	molecular_function	kinase activity
C	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0048029	molecular_function	monosaccharide binding
C	0061621	biological_process	canonical glycolysis
C	0070095	molecular_function	fructose-6-phosphate binding
D	0003872	molecular_function	6-phosphofructokinase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005945	cellular_component	6-phosphofructokinase complex
D	0006002	biological_process	fructose 6-phosphate metabolic process
D	0006096	biological_process	glycolytic process
D	0008443	molecular_function	phosphofructokinase activity
D	0016020	cellular_component	membrane
D	0016208	molecular_function	AMP binding
D	0016301	molecular_function	kinase activity
D	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0048029	molecular_function	monosaccharide binding
D	0061621	biological_process	canonical glycolysis
D	0070095	molecular_function	fructose-6-phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PEP A 401

Chain	Residue
A	ARG21
B	LYS214
B	HIS215
B	HOH626
A	ARG25
A	GLY58
A	ASP59
A	HOH529
B	ARG154
B	GLY185
B	ARG211
B	LYS213

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PEP B 401

Chain	Residue
A	ARG154
A	ARG211
A	LYS213
A	LYS214
A	HIS215
B	ARG21
B	ARG25
B	GLY58
B	ASP59
B	HOH503
B	HOH538

---

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PEP C 401

Chain	Residue
C	ARG21
C	ARG25
C	GLY55
C	GLY58
C	ASP59
C	HOH508
C	HOH549
C	HOH612
D	ARG154
D	GLY185
D	ARG211
D	LYS213
D	LYS214
D	HIS215
D	HOH529

---

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PEP D 401

Chain	Residue
C	ARG154
C	ARG211
C	LYS213
C	LYS214
C	HIS215
C	HOH503
D	ARG21
D	ARG25
D	GLY55
D	GLY58
D	ASP59
D	HOH511
D	HOH571
D	HOH648

---

Functional Information from PROSITE/UniProt

site_id	PS00433
Number of Residues	19
Details	PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtvlGHvQRGGsptafDR

Chain	Residue	Details
A	ARG243-ARG261

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00339

Chain	Residue	Details
A	ASP127
B	ASP127
D	ASP127
C	ASP127

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339

Chain	Residue	Details
C	GLY11
C	GLY102
D	GLY11
D	GLY102
B	GLY102
A	GLY11
A	GLY102
B	GLY11

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:6115424

Chain	Residue	Details
A	ARG162
B	ARG21
B	ASP59
B	ARG72
B	ASP103
B	ARG162
C	ARG21
C	ASP59
C	ARG72
C	ASP103
C	ARG162
D	ARG21
D	ASP59
D	ARG72
D	ASP103
D	ARG162
A	ASP103
A	ARG21
A	ASP59
A	ARG72

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:12390023, ECO:0000269|PubMed:6115424

Chain	Residue	Details
B	THR125
B	MET169
B	GLU222
B	HIS249
C	THR125
C	MET169
C	GLU222
C	HIS249
D	THR125
D	MET169
D	GLU222
D	HIS249
A	HIS249
A	THR125
A	MET169
A	GLU222

---

site_id	SWS_FT_FI5
Number of Residues	16
Details	BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:6115424

Chain	Residue	Details
B	ARG154
B	GLY185
B	ARG211
B	LYS213
C	ARG154
C	GLY185
C	ARG211
C	LYS213
D	ARG154
D	GLY185
D	ARG211
D	LYS213
A	LYS213
A	ARG154
A	GLY185
A	ARG211

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:12390023, ECO:0000269|PubMed:6115424

Chain	Residue	Details
D	ARG243
A	ARG243
B	ARG243
C	ARG243

---