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2V7Z

Crystal structure of the 70-kDa heat shock cognate protein from Rattus norvegicus in post-ATP hydrolysis state

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 Residues14
DetailsBINDING SITE FOR RESIDUE ADP A1383
ChainResidue
ATHR14
ASER275
AGLY339
ASER340
AARG342
APO41384
ATYR15
AASP199
AGLY201
AGLY202
AGLY230
AGLU268
ALYS271
AARG272

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A1384
ChainResidue
AGLY12
ATHR13
ALYS71
AGLU175
AASP199
ATHR204
AADP1383

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP B1383
ChainResidue
BASP10
BTHR14
BTYR15
BASP199
BGLY201
BGLY202
BGLU268
BLYS271
BARG272
BSER275
BGLY339
BSER340
BARG342
BASP366
BPO41384
BHOH2043

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B1384
ChainResidue
BLEU11
BTHR13
BLYS71
BGLU175
BASP199
BTHR204
BADP1383

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 Residues382
DetailsRegion: {"description":"Interaction with BAG1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues32
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P19120","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"UniProtKB","id":"P11142","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P63017","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11142","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11142","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P63017","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kaz
ChainResidueDetails
ALYS71

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kaz
ChainResidueDetails
BLYS71

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PDB entries from 2025-10-08

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