5BPN

Crystal structure of nucleotide-free human Hsp70 NBD double mutant E268Q+R272K.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0016887	molecular_function	ATP hydrolysis activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CL A 401

Chain	Residue
A	THR13
A	LYS71
A	THR204
A	PO4402
A	TRS404

---

site_id	AC2
Number of Residues	8
Details	binding site for residue PO4 A 402

Chain	Residue
A	GLY202
A	THR204
A	CL401
A	TRS404
A	GLY12
A	THR13
A	THR14
A	TYR15

---

site_id	AC3
Number of Residues	3
Details	binding site for residue PO4 A 403

Chain	Residue
A	LEU50
A	ILE51
A	LYS126

---

site_id	AC4
Number of Residues	12
Details	binding site for residue TRS A 404

Chain	Residue
A	ASP10
A	GLY12
A	LYS71
A	GLU175
A	ASP199
A	GLY201
A	VAL337
A	GLY338
A	VAL369
A	CL401
A	PO4402
A	HOH532

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE9-SER16

---

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

Chain	Residue	Details
A	ILE197-LEU210

---

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

Chain	Residue	Details
A	LEU334-LYS348

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"27708256","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---