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5X9U

Crystal structure of group III chaperonin in the open state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005832cellular_componentchaperonin-containing T-complex
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
B0005832cellular_componentchaperonin-containing T-complex
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
C0005832cellular_componentchaperonin-containing T-complex
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
D0005832cellular_componentchaperonin-containing T-complex
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 Residues14
Detailsbinding site for residue ADP A 601
ChainResidue
APRO37
AMET430
APHE461
AMET469
AVAL474
AASP476
AASP87
AGLY88
ATHR89
ATHR90
ATHR91
AGLY389
AGLY390
AGLY391

site_idAC2
Number of Residues12
Detailsbinding site for residue ADP B 601
ChainResidue
BPRO37
BASP87
BGLY88
BTHR89
BTHR90
BTHR91
BGLY389
BGLY390
BMET430
BMET469
BVAL474
BASP476

site_idAC3
Number of Residues11
Detailsbinding site for residue ADP C 601
ChainResidue
CPRO37
CASP87
CGLY88
CTHR90
CTHR91
CILE152
CGLY389
CGLY390
CMET430
CVAL474
CASP476

site_idAC4
Number of Residues12
Detailsbinding site for residue ADP D 601
ChainResidue
DPRO37
DASP87
DGLY88
DTHR89
DTHR90
DTHR91
DGLY389
DGLY390
DMET430
DMET469
DVAL474
DASP476

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 2024-06-12

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