Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5AQI

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
C	0005524	molecular_function	ATP binding
C	0016887	molecular_function	ATP hydrolysis activity
D	0051087	molecular_function	protein-folding chaperone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMS C 1382

Chain	Residue
C	ILE28
C	ILE29
C	ALA30
C	ARG36
C	TYR134
C	HOH2110

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMS A 1382

Chain	Residue
A	ALA30
A	ARG36
A	TYR134
A	GLU27
A	ILE28
A	ILE29

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE DMS A 1383

Chain	Residue
A	ASP206

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1384

Chain	Residue
A	THR13
A	LYS71
A	ARG72
A	ARG76
A	VAL82
A	TYR149

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 1383

Chain	Residue
C	LYS71
C	ARG72
C	ARG76
C	TYR149
C	PHE150

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1385

Chain	Residue
A	TYR15
A	THR37
A	ASP366
A	ADE1388
A	HOH2009
A	HOH2096
A	HOH2097

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 1386

Chain	Residue
A	GLY12
A	THR13
A	SER40
A	ASP69
A	ALA70
A	LYS71
A	SER120
A	VAL123
A	HOH2035

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 1384

Chain	Residue
C	ASN256
C	ARG258
C	ALA259
C	ARG262
C	LEU287
D	LEU218
D	GLN245

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1387

Chain	Residue
A	ASN256
A	ALA259
A	ARG262
A	LEU287
B	GLN245
B	LEU248
B	GOL1263

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 1262

Chain	Residue
B	PHE190
B	HOH2030
C	LEU305
D	GLN154

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 1385

Chain	Residue
C	ARG299
C	GLU303
C	LYS348

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 1386

Chain	Residue
C	LEU11
C	GLY12
C	THR13
C	SER40
C	ASP69
C	ALA70
C	LYS71
C	SER120
C	HOH2046

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 1263

Chain	Residue
A	ARG258
A	GOL1387
A	HOH2077
B	GLN245

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 1264

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

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ADE C 1387

Chain	Residue
C	LYS271
C	ARG272
C	SER275
C	GLY339
C	SER340
C	ARG342
C	HOH2081

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ADE A 1388

Chain	Residue
A	SER275
A	GLY339
A	ARG342
A	GOL1385
A	HOH2069
A	HOH2098

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	382
Details	Region: {"description":"Interaction with BAG1"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	32
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P19120","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
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	4
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	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
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	2
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	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	160
Details	Domain: {"description":"BAG","evidences":[{"source":"PROSITE-ProRule","id":"PRU00369","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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