1ATS

THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS

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	6
Details	BINDING SITE FOR RESIDUE MG A 487

Chain	Residue
A	ADP486
A	HOH507
A	HOH509
A	HOH510
A	HOH511
A	HOH627

---

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ADP A 486

Chain	Residue
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	HOH505
A	HOH507
A	HOH510
A	HOH511
A	HOH521
A	HOH523
A	HOH628
A	THR13
A	THR14
A	TYR15

---

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	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	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"UniProtKB","id":"P11142","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
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_FI6
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","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-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11142","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
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	Annotated By Reference To The Literature 1kaz

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

---