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5X9V

Crystal structure of group III chaperonin in the Closed state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006457biological_processprotein folding
A0016887molecular_functionATP hydrolysis activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051082molecular_functionunfolded protein binding
A0140662molecular_functionATP-dependent protein folding chaperone
B0005524molecular_functionATP binding
B0006457biological_processprotein folding
B0016887molecular_functionATP hydrolysis activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0051082molecular_functionunfolded protein binding
B0140662molecular_functionATP-dependent protein folding chaperone
C0005524molecular_functionATP binding
C0006457biological_processprotein folding
C0016887molecular_functionATP hydrolysis activity
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0051082molecular_functionunfolded protein binding
C0140662molecular_functionATP-dependent protein folding chaperone
D0005524molecular_functionATP binding
D0006457biological_processprotein folding
D0016887molecular_functionATP hydrolysis activity
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0051082molecular_functionunfolded protein binding
D0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue ANP A 601
ChainResidue
ASER34
ATHR89
ATHR90
ATHR91
AILE152
AARG155
AASP373
AGLY389
AGLY390
AMET430
APHE461
ALEU35
AMET469
AASP476
AMG602
AGLY36
APRO37
AASN55
AASP56
AGLY57
AASP87
AGLY88

site_idAC2
Number of Residues2
Detailsbinding site for residue MG A 602
ChainResidue
AASP87
AANP601

site_idAC3
Number of Residues22
Detailsbinding site for residue ANP B 601
ChainResidue
BSER34
BLEU35
BGLY36
BPRO37
BASN55
BASP56
BGLY57
BASP87
BGLY88
BTHR89
BTHR90
BTHR91
BILE152
BARG155
BASP373
BGLY389
BGLY390
BMET430
BPHE461
BVAL474
BASP476
BMG602

site_idAC4
Number of Residues2
Detailsbinding site for residue MG B 602
ChainResidue
BASP87
BANP601

site_idAC5
Number of Residues20
Detailsbinding site for residue ANP C 601
ChainResidue
CSER34
CLEU35
CGLY36
CASN55
CASP56
CGLY57
CASP87
CGLY88
CTHR89
CTHR90
CTHR91
CILE152
CARG155
CASP373
CGLY389
CGLY390
CMET430
CPHE461
CASP476
CMG602

site_idAC6
Number of Residues3
Detailsbinding site for residue MG C 602
ChainResidue
CASP87
CASP373
CANP601

site_idAC7
Number of Residues22
Detailsbinding site for residue ANP D 601
ChainResidue
DSER34
DLEU35
DGLY36
DPRO37
DASN55
DASP56
DGLY57
DASP87
DGLY88
DTHR89
DTHR90
DTHR91
DILE152
DARG155
DASP373
DGLY389
DGLY390
DMET430
DPHE461
DVAL474
DASP476
DMG602

site_idAC8
Number of Residues2
Detailsbinding site for residue MG D 602
ChainResidue
DASP87
DANP601

Functional Information from PROSITE/UniProt
site_idPS00995
Number of Residues9
DetailsTCP1_3 Chaperonins TCP-1 signature 3. QEreVGDGT
ChainResidueDetails
AGLN81-THR89

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PDB entries from 2024-07-10

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