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5AQH

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0140662molecular_functionATP-dependent protein folding chaperone
B0051087molecular_functionprotein-folding chaperone binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZVO A 1382
ChainResidue
AARG272
ASER275
AGLY339
AARG342
AILE343
AHOH2124

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1383
ChainResidue
ALYS71
AGLU175
AASP199
AVAL369
AHOH2003
AHOH2081
AHOH2161
AASP10
ALEU11
AGLY12

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1262
ChainResidue
AALA60
AMET61
BLYS208
BILE211
BGLU255
BHOH2028

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1384
ChainResidue
AASN256
AALA259
AARG262
ASER286
ALEU287
AHOH2109
AHOH2114
BLEU218
BGLN245

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1385
ChainResidue
AGLU255
AASN256
ALYS257
AARG258
AHOH2113
AHOH2163

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1386
ChainResidue
AARG269
AARG272
ATHR273

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1263
ChainResidue
BGLY149
BSER150
BASN151
BGLU155
BASN229
BLYS231
BASP232

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1387
ChainResidue
AASN141
ALEU170
ALYS187
ALEU380
ASER381

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 1388
ChainResidue
AGLY230
AGLU231
AASP234
AGLU268
ALYS271

Functional Information from PROSITE/UniProt
site_idPS00297
Number of Residues8
DetailsHSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS
ChainResidueDetails
AILE9-SER16

site_idPS00329
Number of Residues14
DetailsHSP70_2 Heat shock hsp70 proteins family signature 2. IFDLGGGTfdvSIL
ChainResidueDetails
AILE197-LEU210

site_idPS01036
Number of Residues15
DetailsHSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqK
ChainResidueDetails
AILE334-LYS348

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
BSER152
ALYS71

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P19120
ChainResidueDetails
ATHR14
ATYR15
AGLY202
AGLU268
ALYS271
ASER275
AGLY339

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330
ChainResidueDetails
ASER2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P63017
ChainResidueDetails
ALYS108
ALYS328

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
ASER153

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS246

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P63017
ChainResidueDetails
ALYS319

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER329

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER362

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PDB entries from 2024-07-17

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