5AQU

Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0016887	molecular_function	ATP hydrolysis activity
B	0051087	molecular_function	protein-folding chaperone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1382

Chain	Residue
A	ASN256
A	ARG258
A	ALA259
A	ARG262
A	SER286
A	LEU287
A	GOL1387
B	GLN245

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL B 1261

Chain	Residue
B	LEU148
B	GLY149
B	SER150
B	ASN151
B	GLU155
B	ASN229
B	LYS231
B	ASP232
B	HOH2006
B	PRO147

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 1262

Chain	Residue
B	GLU166
B	LYS236
B	GLY239
B	LEU240
B	LYS243

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1383

Chain	Residue
A	ARG299
A	GLU303
A	PRO344
A	LYS345

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1384

Chain	Residue
A	ARG171
A	THR177
A	ASP214
A	ILE216
A	PHE217
A	GLN376
A	HOH2090

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1385

Chain	Residue
A	THR13
A	ARG72
A	ARG76
A	VAL82
A	ASP86
A	TYR149

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 1263

Chain	Residue
A	GLU289
A	ILE291
B	THR253
B	ASN257

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1386

Chain	Residue
A	ASP152
A	GLN156
A	GLU213
A	ASP214

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1387

Chain	Residue
A	ASN256
A	ARG258
A	GOL1382
A	HOH2112
B	GLN245

---

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE UX0 A 1388

Chain	Residue
A	GLY202
A	GLY230
A	GLU268
A	LYS271
A	ARG272
A	SER275
A	GLY339
A	SER340
A	ARG342
A	HOH2099
A	HOH2129

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS A 1389

Chain	Residue
A	GLU27
A	ILE28
A	ILE29
A	ALA30
A	TYR134

---

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS A 1390

Chain	Residue
A	ASP10
A	GLY12
A	LYS71
A	GLU175
A	ASP199
A	GLY201
A	GLY338
A	HOH2011
A	HOH2167

---

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 1264

Chain	Residue
B	ASP204
B	GLU255
B	ILE258
B	CYS259
B	HOH2050

---

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"}

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":"UniProtKB","id":"P19120","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2010","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Lilla S.","von Kriegsheim A.","Lempens A.","Kolch W.","Bilsland A.E.","Keith W.N."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}

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	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

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

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	80
Details	Domain: {"description":"BAG","evidences":[{"source":"PROSITE-ProRule","id":"PRU00369","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---