Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5AQG

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	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0051087	molecular_function	protein-folding chaperone binding
C	0005524	molecular_function	ATP binding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0051087	molecular_function	protein-folding chaperone binding
E	0005524	molecular_function	ATP binding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
F	0051087	molecular_function	protein-folding chaperone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ZJB A 1382

Chain	Residue
A	GLY201
A	ARG342
A	HOH2078
A	HOH2103
A	HOH2132
A	GLY202
A	GLY230
A	GLU268
A	LYS271
A	ARG272
A	SER275
A	GLY339
A	SER340

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ZJB C 1382

Chain	Residue
C	GLY202
C	GLY230
C	GLU268
C	LYS271
C	ARG272
C	SER275
C	GLY339
C	SER340
C	ARG342
C	HOH2089
C	HOH2114

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ZJB E 1381

Chain	Residue
E	GLY202
E	GLY230
E	GLU268
E	LYS271
E	ARG272
E	SER275
E	GLY339
E	SER340
E	ARG342
E	HOH2036
E	HOH2039
E	HOH2057

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL E 1382

Chain	Residue
E	ASN256
E	ARG262
E	SER286
E	LEU287
E	GOL1383
F	LEU218
F	GLN245

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL E 1383

Chain	Residue
E	SER286
E	TYR288
E	GLU289
E	GLY290
E	GOL1382
F	GLN245

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1383

Chain	Residue
A	ASN256
A	ARG262
A	SER286
A	LEU287
A	HOH2142
B	GLN245

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 1383

Chain	Residue
C	ASN256
C	ARG258
C	ARG262
C	SER286
C	LEU287
D	GLN245

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL F 1261

Chain	Residue
A	LYS248
A	HIS249
A	LYS251
F	GLN187
F	GLN196
F	ASN257

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 1261

Chain	Residue
D	ASN151
D	GLU155
D	ASN229
D	PHE230
D	LYS231
D	ASP232

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1262

Chain	Residue
B	SER150
B	ASN151
B	GLU155
B	ASN229
B	LYS231
B	ASP232

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL F 1262

Chain	Residue
F	ASN151
F	GLU155
F	ASN229
F	LYS231
F	ASP232

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 1384

Chain	Residue
C	HIS249
C	LYS251
C	HOH2096
D	GLN187
D	ASN257

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 1385

Chain	Residue
C	LYS257
C	ARG261

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 1386

Chain	Residue
C	ARG269
C	THR273
C	SER281
C	HOH2120
C	HOH2121
D	ASP222

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 1387

Chain	Residue
C	LYS345
C	ARG299
C	GLU303

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE TRS C 1388

Chain	Residue
C	ASP10
C	GLU175
C	ASP199
C	GLY338
C	VAL369
C	HOH2153

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS A 1384

Chain	Residue
A	ASP10
A	GLU175
A	ASP199
A	VAL337
A	VAL369
A	HOH2132
A	HOH2141

site_id	BC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 1385

Chain	Residue
A	ILE28

site_id	CC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 1389

Chain	Residue
C	ALA30

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	3
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:20068231

Chain	Residue	Details
B	SER152
D	SER152
F	SER152
C	LYS71
E	GLY12
E	LYS71

site_id	SWS_FT_FI2
Number of Residues	21
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P19120

Chain	Residue	Details
A	THR14
C	GLY202
C	GLU268
C	LYS271
C	SER275
C	GLY339
E	THR14
E	TYR15
E	GLY202
E	GLU268
E	LYS271
A	TYR15
E	SER275
E	GLY339
A	GLY202
A	GLU268
A	LYS271
A	SER275
A	GLY339
C	THR14
C	TYR15

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: N-acetylserine => ECO:0000269\|Ref.5, ECO:0000269\|Ref.6, ECO:0007744\|PubMed:19413330

Chain	Residue	Details
A	SER2
C	SER2
E	SER2

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P63017

Chain	Residue	Details
A	LYS108
A	LYS328
C	LYS108
C	LYS328
E	LYS108
E	LYS328

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:17525332

Chain	Residue	Details
A	SER153
C	SER153
E	SER153

site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS246
C	LYS246
E	LYS246

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P63017

Chain	Residue	Details
A	LYS319
C	LYS319
E	LYS319

site_id	SWS_FT_FI8
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER329
C	SER329
E	SER329

site_id	SWS_FT_FI9
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:20068231

Chain	Residue	Details
A	SER362
C	SER362
E	SER362

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)