7KZU

Quasi-intermediate state (Q) of a truncated Hsp70 DnaK fused with a substrate peptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0006457	biological_process	protein folding
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone

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	4
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	2
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	1
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	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---