1HPM

HOW POTASSIUM AFFECTS THE ACTIVITY OF THE MOLECULAR CHAPERONE HSC70. II. POTASSIUM BINDS SPECIFICALLY IN THE ATPASE ACTIVE SITE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 487

Chain	Residue
A	ADP486
A	PO4488
A	K490
A	HOH560
A	HOH561
A	HOH562
A	HOH563

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PO4 A 488

Chain	Residue
A	LYS71
A	PRO147
A	GLU175
A	THR204
A	ADP486
A	MG487
A	K491
A	HOH509
A	HOH545
A	HOH560
A	HOH561
A	HOH562
A	GLY12
A	THR13

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K A 490

Chain	Residue
A	ASP10
A	TYR15
A	ADP486
A	MG487
A	HOH558
A	HOH562
A	HOH563

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 491

Chain	Residue
A	ASP199
A	THR204
A	ASP206
A	PO4488
A	HOH560

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 828

Chain	Residue
A	ASN31
A	ASP32
A	GLN33
A	LYS126

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 523

Chain	Residue
A	TYR183
A	LYS345
A	LYS348
A	HOH537

---

site_id	AC7
Number of Residues	29
Details	BINDING SITE FOR RESIDUE ADP A 486

Chain	Residue
A	GLY12
A	THR13
A	THR14
A	TYR15
A	GLY201
A	GLY202
A	GLY230
A	GLU268
A	LYS271
A	ARG272
A	SER275
A	GLY338
A	GLY339
A	SER340
A	ARG342
A	ASP366
A	MG487
A	PO4488
A	K490
A	HOH545
A	HOH547
A	HOH558
A	HOH560
A	HOH562
A	HOH563
A	HOH564
A	HOH587
A	HOH799
A	HOH1053

---

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. IvLvGGsTRIPkIqK

Chain	Residue	Details
A	ILE334-LYS348

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	191
Details	Region: {"description":"Interaction with BAG1","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PDB","id":"2QWL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QWM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QWN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QWO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QWP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QWQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P63017","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11142","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11142","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P63017","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 7836458, 9585559, 8663302

Chain	Residue	Details
A	LYS71

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 656

Chain	Residue	Details
A	ASP10
A	LYS71	enhance reactivity
A	GLU175
A	ASP199

---