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6ASY

BiP-ATP2

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 PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue GOL A 701
ChainResidue
ALYS353
AASN380
AHOH1216
BGLY430

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 702
ChainResidue
AHOH951
AGLY58
AASN59
AARG60
AILE61
AHOH812

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 703
ChainResidue
AGLU358
ASER385
AARG386
BARG49
BVAL50

site_idAC4
Number of Residues3
Detailsbinding site for residue GOL A 704
ChainResidue
AGLU73
AARG558
BLYS512

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 705
ChainResidue
ALYS340
AGLN343
AHOH844
AHOH1004

site_idAC6
Number of Residues28
Detailsbinding site for residue ATP A 706
ChainResidue
AGLY36
ATHR37
ATHR38
ATYR39
ALYS96
AGLU201
AGLY226
AGLY227
AGLY228
ATHR229
AGLY255
AGLU293
ALYS296
AARG297
ASER300
AGLY363
AGLY364
ASER365
AARG367
AILE368
AHOH815
AHOH841
AHOH871
AHOH882
AHOH939
AHOH1098
AHOH1137
AHOH1231

site_idAC7
Number of Residues6
Detailsbinding site for residue SO4 A 707
ChainResidue
AARG386
AGLY387
AHOH849
AHOH892
BARG60
BASN389

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 A 708
ChainResidue
AHIS265
ALYS326
ALEU330
AHOH964

site_idAC9
Number of Residues6
Detailsbinding site for residue SO4 A 709
ChainResidue
ALYS276
ALYS280
ATYR313
AGLU314
AHOH823
AHOH827

site_idAD1
Number of Residues2
Detailsbinding site for residue SO4 A 710
ChainResidue
AGLN302
AHIS303

site_idAD2
Number of Residues6
Detailsbinding site for residue PO4 A 711
ChainResidue
AASP111
AGLU256
AASP257
AHOH802
AHOH885
AHOH1100

site_idAD3
Number of Residues7
Detailsbinding site for residue PO4 A 712
ChainResidue
ALYS344
AHOH828
AHOH837
AHOH850
BARG466
BASP471
BHOH1032

site_idAD4
Number of Residues6
Detailsbinding site for residue PO4 A 713
ChainResidue
AARG466
AASP471
AHOH819
AHOH860
AHOH1177
BLYS344

site_idAD5
Number of Residues5
Detailsbinding site for residue PO4 A 714
ChainResidue
AGLN182
ALYS185
AHOH830
AHOH918
AHOH953

site_idAD6
Number of Residues9
Detailsbinding site for residue PO4 A 715
ChainResidue
AHOH1015
BGLU89
AGLU25
AVAL27
AHIS167
AASN194
AMET196
AHOH986
AHOH990

site_idAD7
Number of Residues4
Detailsbinding site for residue PO4 A 716
ChainResidue
AGLY387
AILE388
AASN389
BSO4705

site_idAD8
Number of Residues5
Detailsbinding site for residue GOL B 701
ChainResidue
BGLY58
BASN59
BARG60
BILE61
BHOH860

site_idAD9
Number of Residues3
Detailsbinding site for residue GOL B 702
ChainResidue
ALYS512
BGLU73
BARG558

site_idAE1
Number of Residues3
Detailsbinding site for residue GOL B 703
ChainResidue
AGLY430
BLYS353
BASN380

site_idAE2
Number of Residues28
Detailsbinding site for residue ATP B 704
ChainResidue
BGLY36
BTHR37
BTHR38
BTYR39
BLYS96
BGLU201
BGLY226
BGLY227
BGLY228
BTHR229
BGLY255
BGLU293
BLYS296
BARG297
BSER300
BGLY363
BGLY364
BSER365
BARG367
BILE368
BASP391
BHOH803
BHOH841
BHOH899
BHOH900
BHOH944
BHOH1017
BHOH1169

site_idAE3
Number of Residues7
Detailsbinding site for residue SO4 B 705
ChainResidue
AARG60
AASN389
APO4716
BARG386
BGLY387
BHOH947
BHOH970

site_idAE4
Number of Residues6
Detailsbinding site for residue SO4 B 706
ChainResidue
BLYS280
BTYR313
BGLU314
BHOH806
BHOH810
BHOH836

site_idAE5
Number of Residues3
Detailsbinding site for residue SO4 B 707
ChainResidue
BGLN302
BHIS303
BHOH824

site_idAE6
Number of Residues6
Detailsbinding site for residue SO4 B 708
ChainResidue
BHIS265
BLYS326
BHOH1059
BHOH1140
BHOH1206
BHOH1222

site_idAE7
Number of Residues3
Detailsbinding site for residue PO4 B 709
ChainResidue
BGLU256
BASP257
BHOH927

site_idAE8
Number of Residues10
Detailsbinding site for residue PO4 B 710
ChainResidue
AGLU89
BGLU25
BVAL27
BHIS167
BASN194
BHOH864
BHOH874
BHOH975
BHOH1024
BHOH1156

site_idAE9
Number of Residues6
Detailsbinding site for residue PO4 B 711
ChainResidue
BGLN182
BLYS185
BHOH823
BHOH926
BHOH1075
BHOH1224

site_idAF1
Number of Residues7
Detailsbinding site for residue PO4 B 712
ChainResidue
AARG49
AHOH861
BGLU358
BSER385
BARG386
BHOH954
BHOH1159

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

220113

PDB entries from 2024-05-22

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