5NRO

Structure of full-length DnaK with bound J-domain

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0051085	biological_process	chaperone cofactor-dependent protein refolding
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue ATP A 700

Chain	Residue
A	GLY10
A	GLY229
A	GLU267
A	LYS270
A	SER274
A	GLY341
A	GLY342
A	GLN343
A	ARG345
A	MG701
A	HOH802
A	THR11
A	HOH803
A	HOH804
A	THR12
A	ASN13
A	LYS70
A	GLY196
A	GLY197
A	GLY198
A	ALA199

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site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 701

Chain	Residue
A	GLU171
A	ATP700
A	HOH801
A	HOH802
A	HOH803
A	HOH804

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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

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

Chain	Residue	Details
A	VAL192-ILE205

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site_id	PS00636
Number of Residues	20
Details	DNAJ_1 Nt-dnaJ domain signature. FKeIKeaYEvLtDsqkRAAY

Chain	Residue	Details
B	PHE47-TYR66

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

Chain	Residue	Details
A	VAL337-LYS351

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122

Chain	Residue	Details
A	LYS70
A	LYS246
A	LYS359
A	LYS502
A	LYS528
A	LYS587

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site_id	SWS_FT_FI2
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842

Chain	Residue	Details
A	LYS109
A	LYS421
A	LYS556

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:1835085, ECO:0000269|PubMed:8206983

Chain	Residue	Details
A	ALA199

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122

Chain	Residue	Details
A	LYS245
A	LYS304

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