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3CQX

Chaperone Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0140662molecular_functionATP-dependent protein folding chaperone
B0005524molecular_functionATP binding
B0140662molecular_functionATP-dependent protein folding chaperone
C0000774molecular_functionadenyl-nucleotide exchange factor activity
C0051087molecular_functionprotein-folding chaperone binding
D0000774molecular_functionadenyl-nucleotide exchange factor activity
D0051087molecular_functionprotein-folding chaperone binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SCN B 401
ChainResidue
BASN31
BASP32
BGLN33
BTHR38
BASP53
BLYS126

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SCN A 402
ChainResidue
AALA60
AARG258

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SCN A 403
ChainResidue
AGLU303
AARG299

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SCN A 404
ChainResidue
APHE310
ALYS345
ALEU349
BALA81

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SCN A 405
ChainResidue
AASP285
DLYS168
DLYS171
DARG172

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AGLY75
AGLU117

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 502
ChainResidue
ALYS71
AARG72
AILE74
AARG76
AGLN154

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 503
ChainResidue
AALA30
AILE130
AALA133

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA D 504
ChainResidue
AASP285
DCYS142
DGLN167

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 Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY12
ALYS71
BGLY12
BLYS71

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P19120
ChainResidueDetails
ATHR14
BGLY202
BGLU268
BLYS271
BSER275
BGLY339
ATYR15
AGLY202
AGLU268
ALYS271
ASER275
AGLY339
BTHR14
BTYR15

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P11142
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS108
ALYS246
ALYS328
BLYS108
BLYS246
BLYS328

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11142
ChainResidueDetails
ASER153
ASER329
ASER362
BSER153
BSER329
BSER362

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS319
BLYS319

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

225681

PDB entries from 2024-10-02

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