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4H5V

HSC70 NBD with Mg

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AGLY12
AHOH534
AHOH590
AHOH645
ATHR13
ALYS71
AGLU175
ATHR204
AMG402
AHOH501
AHOH503
AHOH504

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
ASO4401
AHOH501
AHOH502
AHOH503
AHOH504
AHOH505

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 403
ChainResidue
ATHR14
ATYR15
AHOH505

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
AARG77
AARG100
AILE297
ATHR298
AARG301
AHOH719
AHOH737

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 405
ChainResidue
AGLU27
AILE28
AARG36
AHOH706

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 406
ChainResidue
ATHR13
ALYS71
AARG72
AARG76
ATYR149
APHE150
AGLN154
ATHR204
ATHR226
AHOH588
AHOH718

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 407
ChainResidue
AASN151
AASP152
ALYS248
AHOH735
AHOH791

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 408
ChainResidue
AASN35
AARG36
ATHR37
AHOH686
AHOH753

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 409
ChainResidue
AASP225
ATHR226

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 410
ChainResidue
AARG262
AHOH587
AHOH650
AHOH677

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 Residues2
DetailsBINDING:
ChainResidueDetails
AGLY12
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 2024-09-11

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