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7N1R

A novel and unique ATP hydrolysis to AMP by a human Hsp70 BiP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005789cellular_componentendoplasmic reticulum membrane
A0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006983biological_processER overload response
A0008180cellular_componentCOP9 signalosome
A0009986cellular_componentcell surface
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0019899molecular_functionenzyme binding
A0019904molecular_functionprotein domain specific binding
A0021589biological_processcerebellum structural organization
A0021680biological_processcerebellar Purkinje cell layer development
A0021762biological_processsubstantia nigra development
A0030335biological_processpositive regulation of cell migration
A0030496cellular_componentmidbody
A0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
A0030968biological_processendoplasmic reticulum unfolded protein response
A0031072molecular_functionheat shock protein binding
A0031204biological_processpost-translational protein targeting to membrane, translocation
A0031333biological_processnegative regulation of protein-containing complex assembly
A0031398biological_processpositive regulation of protein ubiquitination
A0031625molecular_functionubiquitin protein ligase binding
A0032991cellular_componentprotein-containing complex
A0034663cellular_componentendoplasmic reticulum chaperone complex
A0034975biological_processprotein folding in endoplasmic reticulum
A0034976biological_processresponse to endoplasmic reticulum stress
A0035437biological_processmaintenance of protein localization in endoplasmic reticulum
A0036503biological_processERAD pathway
A0042026biological_processprotein refolding
A0042149biological_processcellular response to glucose starvation
A0042470cellular_componentmelanosome
A0043022molecular_functionribosome binding
A0043066biological_processnegative regulation of apoptotic process
A0043231cellular_componentintracellular membrane-bounded organelle
A0044183molecular_functionprotein folding chaperone
A0045296molecular_functioncadherin binding
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0051082molecular_functionunfolded protein binding
A0051085biological_processchaperone cofactor-dependent protein refolding
A0051087molecular_functionprotein-folding chaperone binding
A0051603biological_processproteolysis involved in protein catabolic process
A0051787molecular_functionmisfolded protein binding
A0060904biological_processregulation of protein folding in endoplasmic reticulum
A0070062cellular_componentextracellular exosome
A0071353biological_processcellular response to interleukin-4
A0140662molecular_functionATP-dependent protein folding chaperone
A1903891biological_processregulation of ATF6-mediated unfolded protein response
A1903894biological_processregulation of IRE1-mediated unfolded protein response
A1903895biological_processnegative regulation of IRE1-mediated unfolded protein response
A1903897biological_processregulation of PERK-mediated unfolded protein response
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005783cellular_componentendoplasmic reticulum
B0005788cellular_componentendoplasmic reticulum lumen
B0005789cellular_componentendoplasmic reticulum membrane
B0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006983biological_processER overload response
B0008180cellular_componentCOP9 signalosome
B0009986cellular_componentcell surface
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0019899molecular_functionenzyme binding
B0019904molecular_functionprotein domain specific binding
B0021589biological_processcerebellum structural organization
B0021680biological_processcerebellar Purkinje cell layer development
B0021762biological_processsubstantia nigra development
B0030335biological_processpositive regulation of cell migration
B0030496cellular_componentmidbody
B0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
B0030968biological_processendoplasmic reticulum unfolded protein response
B0031072molecular_functionheat shock protein binding
B0031204biological_processpost-translational protein targeting to membrane, translocation
B0031333biological_processnegative regulation of protein-containing complex assembly
B0031398biological_processpositive regulation of protein ubiquitination
B0031625molecular_functionubiquitin protein ligase binding
B0032991cellular_componentprotein-containing complex
B0034663cellular_componentendoplasmic reticulum chaperone complex
B0034975biological_processprotein folding in endoplasmic reticulum
B0034976biological_processresponse to endoplasmic reticulum stress
B0035437biological_processmaintenance of protein localization in endoplasmic reticulum
B0036503biological_processERAD pathway
B0042026biological_processprotein refolding
B0042149biological_processcellular response to glucose starvation
B0042470cellular_componentmelanosome
B0043022molecular_functionribosome binding
B0043066biological_processnegative regulation of apoptotic process
B0043231cellular_componentintracellular membrane-bounded organelle
B0044183molecular_functionprotein folding chaperone
B0045296molecular_functioncadherin binding
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0051082molecular_functionunfolded protein binding
B0051085biological_processchaperone cofactor-dependent protein refolding
B0051087molecular_functionprotein-folding chaperone binding
B0051603biological_processproteolysis involved in protein catabolic process
B0051787molecular_functionmisfolded protein binding
B0060904biological_processregulation of protein folding in endoplasmic reticulum
B0070062cellular_componentextracellular exosome
B0071353biological_processcellular response to interleukin-4
B0140662molecular_functionATP-dependent protein folding chaperone
B1903891biological_processregulation of ATF6-mediated unfolded protein response
B1903894biological_processregulation of IRE1-mediated unfolded protein response
B1903895biological_processnegative regulation of IRE1-mediated unfolded protein response
B1903897biological_processregulation of PERK-mediated unfolded protein response
Functional Information from PROSITE/UniProt
site_idPS00297
Number of Residues8
DetailsHSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS
ChainResidueDetails
AILE33-SER40

site_idPS00329
Number of Residues14
DetailsHSP70_2 Heat shock hsp70 proteins family signature 2. VFDLGGGTfdvSLL
ChainResidueDetails
AVAL222-LEU235

site_idPS01036
Number of Residues15
DetailsHSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqQ
ChainResidueDetails
AILE359-GLN373

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:21526763
ChainResidueDetails
AGLY36
BGLY364
ALYS96
AGLY227
AGLU293
AGLY364
BGLY36
BLYS96
BGLY227
BGLU293

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06761
ChainResidueDetails
ASER86
BSER86

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P20029
ChainResidueDetails
ALYS125
ALYS213
ALYS326
BLYS125
BLYS213
BLYS326

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P20029
ChainResidueDetails
ATYR160
BTYR160

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DMV8
ChainResidueDetails
ALYS271
BLYS271

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P20029
ChainResidueDetails
ALYS353
BLYS353

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P20029
ChainResidueDetails
ALYS447
BLYS447

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P0DMV8
ChainResidueDetails
AGLN492
BGLN492

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine; alternate => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
ChainResidueDetails
AASN518
BASN518

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
AGLU585
BGLU585

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0007744|PubMed:24129315
ChainResidueDetails
AGLU591
BGLU591

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS352
BLYS352

site_idSWS_FT_FI13
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211
ChainResidueDetails
ALYS353
BLYS353

223166

PDB entries from 2024-07-31

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