Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5E84

ATP-bound state of 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
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005783cellular_componentendoplasmic reticulum
C0005788cellular_componentendoplasmic reticulum lumen
C0005789cellular_componentendoplasmic reticulum membrane
C0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0005925cellular_componentfocal adhesion
C0006983biological_processER overload response
C0008180cellular_componentCOP9 signalosome
C0009986cellular_componentcell surface
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0016887molecular_functionATP hydrolysis activity
C0019899molecular_functionenzyme binding
C0019904molecular_functionprotein domain specific binding
C0021589biological_processcerebellum structural organization
C0021680biological_processcerebellar Purkinje cell layer development
C0021762biological_processsubstantia nigra development
C0030335biological_processpositive regulation of cell migration
C0030496cellular_componentmidbody
C0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
C0030968biological_processendoplasmic reticulum unfolded protein response
C0031072molecular_functionheat shock protein binding
C0031204biological_processpost-translational protein targeting to membrane, translocation
C0031333biological_processnegative regulation of protein-containing complex assembly
C0031398biological_processpositive regulation of protein ubiquitination
C0031625molecular_functionubiquitin protein ligase binding
C0032991cellular_componentprotein-containing complex
C0034663cellular_componentendoplasmic reticulum chaperone complex
C0034975biological_processprotein folding in endoplasmic reticulum
C0034976biological_processresponse to endoplasmic reticulum stress
C0035437biological_processmaintenance of protein localization in endoplasmic reticulum
C0036503biological_processERAD pathway
C0042026biological_processprotein refolding
C0042149biological_processcellular response to glucose starvation
C0042470cellular_componentmelanosome
C0043022molecular_functionribosome binding
C0043066biological_processnegative regulation of apoptotic process
C0043231cellular_componentintracellular membrane-bounded organelle
C0044183molecular_functionprotein folding chaperone
C0045296molecular_functioncadherin binding
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0051082molecular_functionunfolded protein binding
C0051085biological_processchaperone cofactor-dependent protein refolding
C0051087molecular_functionprotein-folding chaperone binding
C0051603biological_processproteolysis involved in protein catabolic process
C0051787molecular_functionmisfolded protein binding
C0060904biological_processregulation of protein folding in endoplasmic reticulum
C0070062cellular_componentextracellular exosome
C0071353biological_processcellular response to interleukin-4
C0140662molecular_functionATP-dependent protein folding chaperone
C1903891biological_processregulation of ATF6-mediated unfolded protein response
C1903894biological_processregulation of IRE1-mediated unfolded protein response
C1903895biological_processnegative regulation of IRE1-mediated unfolded protein response
C1903897biological_processregulation of PERK-mediated unfolded protein response
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005783cellular_componentendoplasmic reticulum
D0005788cellular_componentendoplasmic reticulum lumen
D0005789cellular_componentendoplasmic reticulum membrane
D0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0005925cellular_componentfocal adhesion
D0006983biological_processER overload response
D0008180cellular_componentCOP9 signalosome
D0009986cellular_componentcell surface
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
D0016887molecular_functionATP hydrolysis activity
D0019899molecular_functionenzyme binding
D0019904molecular_functionprotein domain specific binding
D0021589biological_processcerebellum structural organization
D0021680biological_processcerebellar Purkinje cell layer development
D0021762biological_processsubstantia nigra development
D0030335biological_processpositive regulation of cell migration
D0030496cellular_componentmidbody
D0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
D0030968biological_processendoplasmic reticulum unfolded protein response
D0031072molecular_functionheat shock protein binding
D0031204biological_processpost-translational protein targeting to membrane, translocation
D0031333biological_processnegative regulation of protein-containing complex assembly
D0031398biological_processpositive regulation of protein ubiquitination
D0031625molecular_functionubiquitin protein ligase binding
D0032991cellular_componentprotein-containing complex
D0034663cellular_componentendoplasmic reticulum chaperone complex
D0034975biological_processprotein folding in endoplasmic reticulum
D0034976biological_processresponse to endoplasmic reticulum stress
D0035437biological_processmaintenance of protein localization in endoplasmic reticulum
D0036503biological_processERAD pathway
D0042026biological_processprotein refolding
D0042149biological_processcellular response to glucose starvation
D0042470cellular_componentmelanosome
D0043022molecular_functionribosome binding
D0043066biological_processnegative regulation of apoptotic process
D0043231cellular_componentintracellular membrane-bounded organelle
D0044183molecular_functionprotein folding chaperone
D0045296molecular_functioncadherin binding
D0045944biological_processpositive regulation of transcription by RNA polymerase II
D0051082molecular_functionunfolded protein binding
D0051085biological_processchaperone cofactor-dependent protein refolding
D0051087molecular_functionprotein-folding chaperone binding
D0051603biological_processproteolysis involved in protein catabolic process
D0051787molecular_functionmisfolded protein binding
D0060904biological_processregulation of protein folding in endoplasmic reticulum
D0070062cellular_componentextracellular exosome
D0071353biological_processcellular response to interleukin-4
D0140662molecular_functionATP-dependent protein folding chaperone
D1903891biological_processregulation of ATF6-mediated unfolded protein response
D1903894biological_processregulation of IRE1-mediated unfolded protein response
D1903895biological_processnegative regulation of IRE1-mediated unfolded protein response
D1903897biological_processregulation of PERK-mediated unfolded protein response
E0005509molecular_functioncalcium ion binding
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005739cellular_componentmitochondrion
E0005783cellular_componentendoplasmic reticulum
E0005788cellular_componentendoplasmic reticulum lumen
E0005789cellular_componentendoplasmic reticulum membrane
E0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0005925cellular_componentfocal adhesion
E0006983biological_processER overload response
E0008180cellular_componentCOP9 signalosome
E0009986cellular_componentcell surface
E0016020cellular_componentmembrane
E0016787molecular_functionhydrolase activity
E0016887molecular_functionATP hydrolysis activity
E0019899molecular_functionenzyme binding
E0019904molecular_functionprotein domain specific binding
E0021589biological_processcerebellum structural organization
E0021680biological_processcerebellar Purkinje cell layer development
E0021762biological_processsubstantia nigra development
E0030335biological_processpositive regulation of cell migration
E0030496cellular_componentmidbody
E0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
E0030968biological_processendoplasmic reticulum unfolded protein response
E0031072molecular_functionheat shock protein binding
E0031204biological_processpost-translational protein targeting to membrane, translocation
E0031333biological_processnegative regulation of protein-containing complex assembly
E0031398biological_processpositive regulation of protein ubiquitination
E0031625molecular_functionubiquitin protein ligase binding
E0032991cellular_componentprotein-containing complex
E0034663cellular_componentendoplasmic reticulum chaperone complex
E0034975biological_processprotein folding in endoplasmic reticulum
E0034976biological_processresponse to endoplasmic reticulum stress
E0035437biological_processmaintenance of protein localization in endoplasmic reticulum
E0036503biological_processERAD pathway
E0042026biological_processprotein refolding
E0042149biological_processcellular response to glucose starvation
E0042470cellular_componentmelanosome
E0043022molecular_functionribosome binding
E0043066biological_processnegative regulation of apoptotic process
E0043231cellular_componentintracellular membrane-bounded organelle
E0044183molecular_functionprotein folding chaperone
E0045296molecular_functioncadherin binding
E0045944biological_processpositive regulation of transcription by RNA polymerase II
E0051082molecular_functionunfolded protein binding
E0051085biological_processchaperone cofactor-dependent protein refolding
E0051087molecular_functionprotein-folding chaperone binding
E0051603biological_processproteolysis involved in protein catabolic process
E0051787molecular_functionmisfolded protein binding
E0060904biological_processregulation of protein folding in endoplasmic reticulum
E0070062cellular_componentextracellular exosome
E0071353biological_processcellular response to interleukin-4
E0140662molecular_functionATP-dependent protein folding chaperone
E1903891biological_processregulation of ATF6-mediated unfolded protein response
E1903894biological_processregulation of IRE1-mediated unfolded protein response
E1903895biological_processnegative regulation of IRE1-mediated unfolded protein response
E1903897biological_processregulation of PERK-mediated unfolded protein response
F0005509molecular_functioncalcium ion binding
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005739cellular_componentmitochondrion
F0005783cellular_componentendoplasmic reticulum
F0005788cellular_componentendoplasmic reticulum lumen
F0005789cellular_componentendoplasmic reticulum membrane
F0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0005925cellular_componentfocal adhesion
F0006983biological_processER overload response
F0008180cellular_componentCOP9 signalosome
F0009986cellular_componentcell surface
F0016020cellular_componentmembrane
F0016787molecular_functionhydrolase activity
F0016887molecular_functionATP hydrolysis activity
F0019899molecular_functionenzyme binding
F0019904molecular_functionprotein domain specific binding
F0021589biological_processcerebellum structural organization
F0021680biological_processcerebellar Purkinje cell layer development
F0021762biological_processsubstantia nigra development
F0030335biological_processpositive regulation of cell migration
F0030496cellular_componentmidbody
F0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
F0030968biological_processendoplasmic reticulum unfolded protein response
F0031072molecular_functionheat shock protein binding
F0031204biological_processpost-translational protein targeting to membrane, translocation
F0031333biological_processnegative regulation of protein-containing complex assembly
F0031398biological_processpositive regulation of protein ubiquitination
F0031625molecular_functionubiquitin protein ligase binding
F0032991cellular_componentprotein-containing complex
F0034663cellular_componentendoplasmic reticulum chaperone complex
F0034975biological_processprotein folding in endoplasmic reticulum
F0034976biological_processresponse to endoplasmic reticulum stress
F0035437biological_processmaintenance of protein localization in endoplasmic reticulum
F0036503biological_processERAD pathway
F0042026biological_processprotein refolding
F0042149biological_processcellular response to glucose starvation
F0042470cellular_componentmelanosome
F0043022molecular_functionribosome binding
F0043066biological_processnegative regulation of apoptotic process
F0043231cellular_componentintracellular membrane-bounded organelle
F0044183molecular_functionprotein folding chaperone
F0045296molecular_functioncadherin binding
F0045944biological_processpositive regulation of transcription by RNA polymerase II
F0051082molecular_functionunfolded protein binding
F0051085biological_processchaperone cofactor-dependent protein refolding
F0051087molecular_functionprotein-folding chaperone binding
F0051603biological_processproteolysis involved in protein catabolic process
F0051787molecular_functionmisfolded protein binding
F0060904biological_processregulation of protein folding in endoplasmic reticulum
F0070062cellular_componentextracellular exosome
F0071353biological_processcellular response to interleukin-4
F0140662molecular_functionATP-dependent protein folding chaperone
F1903891biological_processregulation of ATF6-mediated unfolded protein response
F1903894biological_processregulation of IRE1-mediated unfolded protein response
F1903895biological_processnegative regulation of IRE1-mediated unfolded protein response
F1903897biological_processregulation of PERK-mediated unfolded protein response
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue ATP A 801
ChainResidue
AGLY36
AALA229
AGLY255
AGLU293
ALYS296
AARG297
ASER300
AGLY363
AGLY364
ASER365
AARG367
ATHR37
AILE368
AZN802
ATHR38
ATYR39
ALYS96
AGLU201
AGLY226
AGLY227
AGLY228

site_idAC2
Number of Residues2
Detailsbinding site for residue ZN A 802
ChainResidue
AASP34
AATP801

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 803
ChainResidue
AASP608
AASP611
CASP608
CASP611
CMG803

site_idAC4
Number of Residues3
Detailsbinding site for residue MG A 804
ChainResidue
AGLU316
CGLU310
CASP317

site_idAC5
Number of Residues3
Detailsbinding site for residue MG A 805
ChainResidue
AGLU310
AASP317
CGLU316

site_idAC6
Number of Residues3
Detailsbinding site for residue ZN A 806
ChainResidue
AGLU201
AASP224
AASP231

site_idAC7
Number of Residues1
Detailsbinding site for residue ZN A 807
ChainResidue
AASP238

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 A 808
ChainResidue
AGLU25
AVAL27
AHIS167
AASN194

site_idAC9
Number of Residues24
Detailsbinding site for residue ATP B 801
ChainResidue
BASP34
BGLY36
BTHR37
BTHR38
BTYR39
BLYS96
BGLU201
BGLY226
BGLY227
BGLY228
BALA229
BGLY255
BGLU293
BLYS296
BARG297
BSER300
BGLY363
BGLY364
BSER365
BARG367
BILE368
BZN802
BZN803
BHOH903

site_idAD1
Number of Residues3
Detailsbinding site for residue ZN B 802
ChainResidue
BASP34
BATP801
BHOH903

site_idAD2
Number of Residues5
Detailsbinding site for residue ZN B 803
ChainResidue
BGLU201
BASP224
BALA229
BASP231
BATP801

site_idAD3
Number of Residues3
Detailsbinding site for residue MG B 804
ChainResidue
BASP608
BASP611
DASP606

site_idAD4
Number of Residues3
Detailsbinding site for residue MG B 805
ChainResidue
BGLU310
BASP317
FGLU314

site_idAD5
Number of Residues2
Detailsbinding site for residue MG B 806
ChainResidue
BGLU316
FGLU316

site_idAD6
Number of Residues1
Detailsbinding site for residue ZN B 807
ChainResidue
BASP238

site_idAD7
Number of Residues3
Detailsbinding site for residue SO4 B 808
ChainResidue
BGLU25
BHIS167
BASN194

site_idAD8
Number of Residues23
Detailsbinding site for residue ATP C 801
ChainResidue
CARG297
CSER300
CGLY363
CGLY364
CSER365
CARG367
CILE368
CASP391
CZN802
CHOH901
CGLY36
CTHR37
CTHR38
CTYR39
CLYS96
CGLU201
CGLY226
CGLY227
CGLY228
CALA229
CGLY255
CGLU293
CLYS296

site_idAD9
Number of Residues3
Detailsbinding site for residue ZN C 802
ChainResidue
CASP34
CATP801
CHOH901

site_idAE1
Number of Residues5
Detailsbinding site for residue MG C 803
ChainResidue
AASP608
AASP611
AMG803
CASP608
CASP611

site_idAE2
Number of Residues3
Detailsbinding site for residue ZN C 804
ChainResidue
CGLU201
CASP224
CASP231

site_idAE3
Number of Residues1
Detailsbinding site for residue ZN C 805
ChainResidue
CASP238

site_idAE4
Number of Residues4
Detailsbinding site for residue SO4 C 806
ChainResidue
CGLU25
CVAL27
CHIS167
CASN194

site_idAE5
Number of Residues22
Detailsbinding site for residue ATP D 801
ChainResidue
DGLY36
DTHR37
DTHR38
DTYR39
DLYS96
DGLU201
DGLY226
DGLY227
DGLY228
DALA229
DGLY255
DGLU293
DLYS296
DARG297
DSER300
DGLY363
DGLY364
DSER365
DARG367
DILE368
DZN802
DHOH901

site_idAE6
Number of Residues3
Detailsbinding site for residue ZN D 802
ChainResidue
DASP34
DATP801
DHOH901

site_idAE7
Number of Residues3
Detailsbinding site for residue MG D 803
ChainResidue
BLYS550
DASP608
DASP611

site_idAE8
Number of Residues3
Detailsbinding site for residue MG D 804
ChainResidue
DGLU316
EGLU310
EASP317

site_idAE9
Number of Residues3
Detailsbinding site for residue MG D 805
ChainResidue
DGLU310
DASP317
EGLU316

site_idAF1
Number of Residues3
Detailsbinding site for residue ZN D 806
ChainResidue
DGLU201
DASP224
DASP231

site_idAF2
Number of Residues1
Detailsbinding site for residue ZN D 807
ChainResidue
DASP238

site_idAF3
Number of Residues4
Detailsbinding site for residue SO4 D 808
ChainResidue
DGLU25
DVAL27
DHIS167
DASN194

site_idAF4
Number of Residues24
Detailsbinding site for residue ATP E 801
ChainResidue
EGLY36
ETHR37
ETHR38
ETYR39
ELYS96
EGLU201
EGLY226
EGLY227
EGLY228
EALA229
EGLY255
EGLU293
ELYS296
EARG297
ESER300
EGLY363
EGLY364
ESER365
EARG367
EILE368
EASP391
EZN803
EZN804
EHOH903

site_idAF5
Number of Residues3
Detailsbinding site for residue MG E 802
ChainResidue
EASP608
EASP611
FLYS550

site_idAF6
Number of Residues4
Detailsbinding site for residue ZN E 803
ChainResidue
EGLU201
EASP224
EASP231
EATP801

site_idAF7
Number of Residues3
Detailsbinding site for residue ZN E 804
ChainResidue
EASP34
EATP801
EHOH903

site_idAF8
Number of Residues1
Detailsbinding site for residue ZN E 805
ChainResidue
EASP238

site_idAF9
Number of Residues3
Detailsbinding site for residue SO4 E 806
ChainResidue
EGLU25
EHIS167
EASN194

site_idAG1
Number of Residues23
Detailsbinding site for residue ATP F 801
ChainResidue
FASP34
FGLY36
FTHR37
FTHR38
FTYR39
FLYS96
FGLU201
FGLY226
FGLY227
FGLY228
FALA229
FGLY255
FGLU293
FLYS296
FARG297
FSER300
FGLY363
FGLY364
FSER365
FARG367
FILE368
FZN802
FHOH901

site_idAG2
Number of Residues3
Detailsbinding site for residue ZN F 802
ChainResidue
FASP34
FATP801
FHOH901

site_idAG3
Number of Residues3
Detailsbinding site for residue MG F 803
ChainResidue
EASP606
FASP608
FASP611

site_idAG4
Number of Residues3
Detailsbinding site for residue ZN F 804
ChainResidue
FGLU201
FASP224
FASP231

site_idAG5
Number of Residues1
Detailsbinding site for residue ZN F 805
ChainResidue
FASP238

site_idAG6
Number of Residues4
Detailsbinding site for residue SO4 F 806
ChainResidue
FGLU25
FVAL27
FHIS167
FASN194

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. VFDLGGGAfdvSLL
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 Residues30
DetailsBINDING: BINDING => ECO:0000269|PubMed:21526763
ChainResidueDetails
AGLY36
BGLY364
CGLY36
CLYS96
CGLY227
CGLU293
CGLY364
DGLY36
DLYS96
DGLY227
DGLU293
ALYS96
DGLY364
EGLY36
ELYS96
EGLY227
EGLU293
EGLY364
FGLY36
FLYS96
FGLY227
FGLU293
AGLY227
FGLY364
AGLU293
AGLY364
BGLY36
BLYS96
BGLY227
BGLU293

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06761
ChainResidueDetails
ASER86
BSER86
CSER86
DSER86
ESER86
FSER86

site_idSWS_FT_FI3
Number of Residues18
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P20029
ChainResidueDetails
ALYS125
DLYS125
DLYS213
DLYS326
ELYS125
ELYS213
ELYS326
FLYS125
FLYS213
FLYS326
ALYS213
ALYS326
BLYS125
BLYS213
BLYS326
CLYS125
CLYS213
CLYS326

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P20029
ChainResidueDetails
ATYR160
BTYR160
CTYR160
DTYR160
ETYR160
FTYR160

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DMV8
ChainResidueDetails
ALYS271
BLYS271
CLYS271
DLYS271
ELYS271
FLYS271

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P20029
ChainResidueDetails
ALYS353
BLYS353
CLYS353
DLYS353
ELYS353
FLYS353

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P20029
ChainResidueDetails
ALYS447
BLYS447
CLYS447
DLYS447
ELYS447
FLYS447

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P0DMV8
ChainResidueDetails
AGLN492
BGLN492
CGLN492
DGLN492
EGLN492
FGLN492

site_idSWS_FT_FI9
Number of Residues6
DetailsMOD_RES: Phosphothreonine; alternate => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
ChainResidueDetails
AASN518
BASN518
CASN518
DASN518
EASN518
FASN518

site_idSWS_FT_FI10
Number of Residues6
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
AGLU585
BGLU585
CGLU585
DGLU585
EGLU585
FGLU585

site_idSWS_FT_FI11
Number of Residues6
DetailsMOD_RES: N6-methyllysine => ECO:0007744|PubMed:24129315
ChainResidueDetails
AGLU591
BGLU591
CGLU591
DGLU591
EGLU591
FGLU591

site_idSWS_FT_FI12
Number of Residues6
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
CLYS352
DLYS352
ELYS352
FLYS352

site_idSWS_FT_FI13
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211
ChainResidueDetails
ELYS353
FLYS353
ALYS353
BLYS353
CLYS353
DLYS353

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon