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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5AQF

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ADN A 1382

Chain	Residue
A	GLY202
A	ILE343
A	HOH2250
A	HOH2300
A	HOH2384
A	HOH2391
A	GLY230
A	GLU268
A	LYS271
A	ARG272
A	SER275
A	GLY339
A	SER340
A	ARG342

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADN C 1382

Chain	Residue
C	GLY202
C	GLY230
C	GLU268
C	LYS271
C	ARG272
C	SER275
C	GLY339
C	SER340
C	ARG342
C	ILE343
C	HOH2207
C	HOH2245
C	HOH2336
C	HOH2342
C	HOH2343

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1383

Chain	Residue
A	ASN256
A	ARG258
A	ALA259
A	ARG262
A	SER286
A	LEU287
A	HOH2282
B	GLN245

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 1383

Chain	Residue
C	ASN256
C	ARG258
C	ALA259
C	ARG262
C	SER286
C	LEU287
D	GLN245

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 1262

Chain	Residue
A	HIS249
A	LYS251
B	GLN187
B	LEU200
B	ASN257

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1384

Chain	Residue
A	GLU27
A	ILE28
A	ALA30
A	ARG36
A	TYR134
A	HOH2038
A	HOH2393

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1385

Chain	Residue
A	THR13
A	LYS71
A	ARG76
A	TYR149
A	PHE150
A	HOH2091

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL C 1384

Chain	Residue
C	THR13
C	LYS71
C	ARG72
C	ARG76
C	VAL82
C	TYR149
C	PHE150
C	HOH2017
C	HOH2068
C	HOH2071
C	HOH2140

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1263

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

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 1261

Chain	Residue
C	GOL1385
D	SER150
D	ASN151
D	GLU155
D	ASN229
D	LYS231
D	ASP232

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 1264

Chain	Residue
B	ALA246
B	ALA246
B	PHE247
B	GLU250
B	HOH2089
B	HOH2090
B	HOH2092
B	HOH2095

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1265

Chain	Residue
B	HOH2096
B	GLN245
B	ALA246
B	GLU250
B	THR253
B	HOH2089

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1386

Chain	Residue
A	ILE181
A	ALA182
A	TYR371

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 1385

Chain	Residue
C	LYS246
C	LYS250
C	LYS251
C	ASP252
D	ASN151
D	ASP232
D	GOL1261
D	HOH2019

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRS A 1387

Chain	Residue
A	ASP10
A	GLY12
A	LYS71
A	GLU175
A	ASP199
A	VAL369
A	HOH2018
A	HOH2381

site_id	BC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS C 1386

Chain	Residue
C	ASP10
C	LYS71
C	GLU175
C	ASP199
C	VAL337
C	GLY338
C	VAL369
C	HOH2069
C	HOH2334
C	HOH2344

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	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:20068231

Chain	Residue	Details
B	SER152
D	SER152
C	GLY12
C	LYS71

site_id	SWS_FT_FI2
Number of Residues	14
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P19120

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

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0000269\|Ref.5, ECO:0000269\|Ref.6, ECO:0007744\|PubMed:19413330

Chain	Residue	Details
A	SER2
C	SER2

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P63017

Chain	Residue	Details
A	LYS108
A	LYS328
C	LYS108
C	LYS328

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:17525332

Chain	Residue	Details
A	SER153
C	SER153

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS246
C	LYS246

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P63017

Chain	Residue	Details
A	LYS319
C	LYS319

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER329
C	SER329

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:20068231

Chain	Residue	Details
A	SER362
C	SER362

218853

PDB entries from 2024-04-24

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