Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7KRT

Restraining state of a truncated Hsp70 DnaK

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 PROSITE/UniProt

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

Chain	Residue	Details
A	ILE7-SER14

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

Chain	Residue	Details
A	VAL192-ILE205

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

Chain	Residue	Details
A	VAL337-LYS351

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
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	12
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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)