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6B1M

Disrupted hydrogen bond network impairs ATPase activity in an Hsc70 cysteine mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0140662molecular_functionATP-dependent protein folding chaperone
B0005524molecular_functionATP binding
B0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues30
Detailsbinding site for residue ANP B 401
ChainResidue
BGLY12
BGLY230
BGLU268
BLYS271
BARG272
BSER275
BGLY338
BGLY339
BSER340
BARG342
BASP366
BTHR13
BMG402
BHOH529
BHOH541
BHOH561
BHOH565
BHOH585
BHOH628
BHOH636
BHOH638
BHOH642
BTHR14
BHOH762
BTYR15
BTRP17
BGLY201
BGLY202
BGLY203
BTHR204

site_idAC2
Number of Residues6
Detailsbinding site for residue MG B 402
ChainResidue
BASP10
BANP401
BHOH529
BHOH628
BHOH716
BHOH830

site_idAC3
Number of Residues29
Detailsbinding site for residue ANP A 401
ChainResidue
AGLY12
ATHR13
ATHR14
ATYR15
ATRP17
AGLY201
AGLY202
AGLY203
ATHR204
AGLY230
AGLU268
ALYS271
AARG272
ASER275
AGLY338
AGLY339
ASER340
AARG342
AILE343
AASP366
AMG402
AHOH553
AHOH557
AHOH572
AHOH603
AHOH625
AHOH627
AHOH641
AHOH772

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 402
ChainResidue
AASP10
AANP401
AHOH603
AHOH641
AHOH763
AHOH766

site_idAC5
Number of Residues10
Detailsbinding site for residue GOL A 403
ChainResidue
AASP186
AGLY190
AALA191
AGLU213
AASP214
AGLY215
AGOL404
AHOH556
AHOH671
AHOH712

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL A 404
ChainResidue
AVAL189
AGLY190
AGOL403
AHOH540
AHOH556

Functional Information from PROSITE/UniProt
site_idPS00297
Number of Residues8
DetailsHSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS
ChainResidueDetails
BILE9-SER16

site_idPS00329
Number of Residues14
DetailsHSP70_2 Heat shock hsp70 proteins family signature 2. IFDLGGGTfdvSIL
ChainResidueDetails
BILE197-LEU210

site_idPS01036
Number of Residues15
DetailsHSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqK
ChainResidueDetails
BILE334-LYS348

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BGLY12
BLYS71
AGLY12
ALYS71

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P19120
ChainResidueDetails
BTHR14
AGLY202
AGLU268
ALYS271
ASER275
AGLY339
BTYR15
BGLY202
BGLU268
BLYS271
BSER275
BGLY339
ATHR14
ATYR15

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P63017
ChainResidueDetails
BLYS108
BLYS328
ALYS108
ALYS328

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
BSER153
ASER153

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS246
ALYS246

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P63017
ChainResidueDetails
BLYS319
ALYS319

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER329
ASER329

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
BSER362
ASER362

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PDB entries from 2024-09-25

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