7KRW

Stimulating state of near full-length Hsp70 DnaK fused with a substrate peptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006260	biological_process	DNA replication
A	0006457	biological_process	protein folding
A	0008270	molecular_function	zinc ion binding
A	0009408	biological_process	response to heat
A	0016020	cellular_component	membrane
A	0016234	cellular_component	inclusion body
A	0016887	molecular_function	ATP hydrolysis activity
A	0016989	molecular_function	sigma factor antagonist activity
A	0031072	molecular_function	heat shock protein binding
A	0032991	cellular_component	protein-containing complex
A	0034620	biological_process	cellular response to unfolded protein
A	0042026	biological_process	protein refolding
A	0043335	biological_process	protein unfolding
A	0043531	molecular_function	ADP binding
A	0044183	molecular_function	protein folding chaperone
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0051082	molecular_function	unfolded protein binding
A	0051087	molecular_function	protein-folding chaperone binding
A	0065003	biological_process	protein-containing complex assembly
A	0140662	molecular_function	ATP-dependent protein folding chaperone
A	1990169	biological_process	stress response to copper ion
B	0000166	molecular_function	nucleotide binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006260	biological_process	DNA replication
B	0006457	biological_process	protein folding
B	0008270	molecular_function	zinc ion binding
B	0009408	biological_process	response to heat
B	0016020	cellular_component	membrane
B	0016234	cellular_component	inclusion body
B	0016887	molecular_function	ATP hydrolysis activity
B	0016989	molecular_function	sigma factor antagonist activity
B	0031072	molecular_function	heat shock protein binding
B	0032991	cellular_component	protein-containing complex
B	0034620	biological_process	cellular response to unfolded protein
B	0042026	biological_process	protein refolding
B	0043335	biological_process	protein unfolding
B	0043531	molecular_function	ADP binding
B	0044183	molecular_function	protein folding chaperone
B	0045892	biological_process	negative regulation of DNA-templated transcription
B	0051082	molecular_function	unfolded protein binding
B	0051087	molecular_function	protein-folding chaperone binding
B	0065003	biological_process	protein-containing complex assembly
B	0140662	molecular_function	ATP-dependent protein folding chaperone
B	1990169	biological_process	stress response to copper ion
C	0000166	molecular_function	nucleotide binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006260	biological_process	DNA replication
C	0006457	biological_process	protein folding
C	0008270	molecular_function	zinc ion binding
C	0009408	biological_process	response to heat
C	0016020	cellular_component	membrane
C	0016234	cellular_component	inclusion body
C	0016887	molecular_function	ATP hydrolysis activity
C	0016989	molecular_function	sigma factor antagonist activity
C	0031072	molecular_function	heat shock protein binding
C	0032991	cellular_component	protein-containing complex
C	0034620	biological_process	cellular response to unfolded protein
C	0042026	biological_process	protein refolding
C	0043335	biological_process	protein unfolding
C	0043531	molecular_function	ADP binding
C	0044183	molecular_function	protein folding chaperone
C	0045892	biological_process	negative regulation of DNA-templated transcription
C	0051082	molecular_function	unfolded protein binding
C	0051087	molecular_function	protein-folding chaperone binding
C	0065003	biological_process	protein-containing complex assembly
C	0140662	molecular_function	ATP-dependent protein folding chaperone
C	1990169	biological_process	stress response to copper ion
D	0000166	molecular_function	nucleotide binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006260	biological_process	DNA replication
D	0006457	biological_process	protein folding
D	0008270	molecular_function	zinc ion binding
D	0009408	biological_process	response to heat
D	0016020	cellular_component	membrane
D	0016234	cellular_component	inclusion body
D	0016887	molecular_function	ATP hydrolysis activity
D	0016989	molecular_function	sigma factor antagonist activity
D	0031072	molecular_function	heat shock protein binding
D	0032991	cellular_component	protein-containing complex
D	0034620	biological_process	cellular response to unfolded protein
D	0042026	biological_process	protein refolding
D	0043335	biological_process	protein unfolding
D	0043531	molecular_function	ADP binding
D	0044183	molecular_function	protein folding chaperone
D	0045892	biological_process	negative regulation of DNA-templated transcription
D	0051082	molecular_function	unfolded protein binding
D	0051087	molecular_function	protein-folding chaperone binding
D	0065003	biological_process	protein-containing complex assembly
D	0140662	molecular_function	ATP-dependent protein folding chaperone
D	1990169	biological_process	stress response to copper ion

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue ATP C 701

Chain	Residue
C	GLY10
C	ILE271
C	SER274
C	GLY341
C	GLY342
C	GLN343
C	ARG345
C	THR11
C	THR12
C	LYS70
C	GLU171
C	GLY196
C	GLY197
C	GLY198
C	LYS270

---

site_id	AC2
Number of Residues	17
Details	binding site for residue ATP B 701

Chain	Residue
B	ASP8
B	GLY10
B	THR11
B	THR12
B	ASN13
B	LYS70
B	GLU171
B	ASP194
B	GLY196
B	GLY197
B	GLY198
B	ALA199
B	GLY229
B	ILE271
B	SER274
B	GLY342
B	ARG345

---

site_id	AC3
Number of Residues	15
Details	binding site for residue ATP A 701

Chain	Residue
A	LEU9
A	GLY10
A	THR11
A	THR12
A	ASN13
A	LYS70
A	GLU171
A	GLY197
A	LYS270
A	SER274
A	GLY341
A	GLY342
A	GLN343
A	ARG345
A	PRO367

---

site_id	AC4
Number of Residues	17
Details	binding site for residue ATP D 701

Chain	Residue
D	ASP8
D	GLY10
D	THR11
D	THR12
D	ASN13
D	LYS70
D	GLU171
D	GLY196
D	GLY197
D	GLY198
D	ALA199
D	GLU267
D	ILE271
D	GLY342
D	GLN343
D	ARG345
D	ASP368

---

Functional Information from PROSITE/UniProt

site_id	PS00297
Number of Residues	8
Details	HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTnS

Chain	Residue	Details
C	ILE7-SER14

---

site_id	PS00329
Number of Residues	14
Details	HSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGAfdiSII

Chain	Residue	Details
C	VAL192-ILE205

---

site_id	PS01036
Number of Residues	15
Details	HSP70_3 Heat shock hsp70 proteins family signature 3. ViLvGGqTRMPmVqK

Chain	Residue	Details
C	VAL337-LYS351

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	21
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"1835085","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8206983","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---