Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5W74

Crystal Structure of the Group II Chaperonin from Methanococcus Maripaludis D386ADeltaLid Mutant in the Open, ADP-Bound State

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006457biological_processprotein folding
A0016787molecular_functionhydrolase activity
A0016853molecular_functionisomerase activity
A0016887molecular_functionATP hydrolysis activity
A0032991cellular_componentprotein-containing complex
A0051082molecular_functionunfolded protein binding
A0140662molecular_functionATP-dependent protein folding chaperone
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006457biological_processprotein folding
B0016787molecular_functionhydrolase activity
B0016853molecular_functionisomerase activity
B0016887molecular_functionATP hydrolysis activity
B0032991cellular_componentprotein-containing complex
B0051082molecular_functionunfolded protein binding
B0140662molecular_functionATP-dependent protein folding chaperone
C0000166molecular_functionnucleotide binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006457biological_processprotein folding
C0016787molecular_functionhydrolase activity
C0016853molecular_functionisomerase activity
C0016887molecular_functionATP hydrolysis activity
C0032991cellular_componentprotein-containing complex
C0051082molecular_functionunfolded protein binding
C0140662molecular_functionATP-dependent protein folding chaperone
D0000166molecular_functionnucleotide binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006457biological_processprotein folding
D0016787molecular_functionhydrolase activity
D0016853molecular_functionisomerase activity
D0016887molecular_functionATP hydrolysis activity
D0032991cellular_componentprotein-containing complex
D0051082molecular_functionunfolded protein binding
D0140662molecular_functionATP-dependent protein folding chaperone
E0000166molecular_functionnucleotide binding
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0006457biological_processprotein folding
E0016787molecular_functionhydrolase activity
E0016853molecular_functionisomerase activity
E0016887molecular_functionATP hydrolysis activity
E0032991cellular_componentprotein-containing complex
E0051082molecular_functionunfolded protein binding
E0140662molecular_functionATP-dependent protein folding chaperone
F0000166molecular_functionnucleotide binding
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0006457biological_processprotein folding
F0016787molecular_functionhydrolase activity
F0016853molecular_functionisomerase activity
F0016887molecular_functionATP hydrolysis activity
F0032991cellular_componentprotein-containing complex
F0051082molecular_functionunfolded protein binding
F0140662molecular_functionATP-dependent protein folding chaperone
G0000166molecular_functionnucleotide binding
G0005524molecular_functionATP binding
G0005737cellular_componentcytoplasm
G0006457biological_processprotein folding
G0016787molecular_functionhydrolase activity
G0016853molecular_functionisomerase activity
G0016887molecular_functionATP hydrolysis activity
G0032991cellular_componentprotein-containing complex
G0051082molecular_functionunfolded protein binding
G0140662molecular_functionATP-dependent protein folding chaperone
H0000166molecular_functionnucleotide binding
H0005524molecular_functionATP binding
H0005737cellular_componentcytoplasm
H0006457biological_processprotein folding
H0016787molecular_functionhydrolase activity
H0016853molecular_functionisomerase activity
H0016887molecular_functionATP hydrolysis activity
H0032991cellular_componentprotein-containing complex
H0051082molecular_functionunfolded protein binding
H0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue ADP A 600
ChainResidue
ALEU39
AGLY405
ALEU473
AASN474
AVAL488
AGLU490
ALYS495
AMG601
AGLY40
AASP91
AGLY92
ATHR94
ATHR95
AGLY160
AGLY403
AGLY404

site_idAC2
Number of Residues2
Detailsbinding site for residue MG A 601
ChainResidue
ATHR94
AADP600

site_idAC3
Number of Residues14
Detailsbinding site for residue ADP B 600
ChainResidue
BLEU39
BASP91
BGLY92
BTHR93
BTHR94
BTHR95
BTHR156
BGLY160
BGLY403
BGLY404
BVAL488
BGLU490
BLYS495
BMG601

site_idAC4
Number of Residues2
Detailsbinding site for residue MG B 601
ChainResidue
BASP91
BADP600

site_idAC5
Number of Residues17
Detailsbinding site for residue ADP C 600
ChainResidue
CTHR38
CLEU39
CGLY40
CPRO41
CASP91
CGLY92
CTHR93
CTHR94
CTHR95
CTHR156
CTHR159
CGLY160
CGLY404
CLEU473
CPHE476
CGLU490
CMG601

site_idAC6
Number of Residues3
Detailsbinding site for residue MG C 601
ChainResidue
CASP91
CSER157
CADP600

site_idAC7
Number of Residues14
Detailsbinding site for residue ADP D 600
ChainResidue
DLEU39
DGLY40
DPRO41
DASP91
DGLY92
DTHR93
DTHR94
DTHR95
DTHR156
DGLY160
DGLY404
DGLU490
DLYS495
DMG601

site_idAC8
Number of Residues3
Detailsbinding site for residue MG D 601
ChainResidue
DASP91
DSER157
DADP600

site_idAC9
Number of Residues15
Detailsbinding site for residue ADP E 600
ChainResidue
ELEU39
EGLY40
EPRO41
EASP91
EGLY92
ETHR94
ETHR95
EGLY160
EGLY403
EGLY404
EGLY405
ELEU473
EGLU490
ELYS495
EMG601

site_idAD1
Number of Residues2
Detailsbinding site for residue MG E 601
ChainResidue
EASP91
EADP600

site_idAD2
Number of Residues17
Detailsbinding site for residue ADP F 600
ChainResidue
FGLY404
FLEU473
FPHE476
FGLU490
FLYS495
FMG601
FTHR38
FLEU39
FGLY40
FPRO41
FASP91
FGLY92
FTHR94
FTHR95
FTHR156
FGLY160
FGLY403

site_idAD3
Number of Residues3
Detailsbinding site for residue MG F 601
ChainResidue
FASP91
FSER157
FADP600

site_idAD4
Number of Residues15
Detailsbinding site for residue ADP G 600
ChainResidue
GLEU39
GGLY40
GPRO41
GASP91
GGLY92
GTHR94
GTHR95
GGLY160
GGLY403
GGLY404
GLEU473
GVAL488
GGLU490
GLYS495
GMG601

site_idAD5
Number of Residues2
Detailsbinding site for residue MG G 601
ChainResidue
GASP91
GADP600

site_idAD6
Number of Residues18
Detailsbinding site for residue ADP H 600
ChainResidue
HTHR38
HLEU39
HGLY40
HPRO41
HASP91
HGLY92
HTHR93
HTHR94
HTHR95
HTHR156
HTHR159
HGLY160
HGLY404
HPHE476
HVAL488
HGLU490
HLYS495
HMG601

site_idAD7
Number of Residues3
Detailsbinding site for residue MG H 601
ChainResidue
HASP91
HSER157
HADP600

Functional Information from PROSITE/UniProt
site_idPS00750
Number of Residues13
DetailsTCP1_1 Chaperonins TCP-1 signature 1. RStLGPkGmdKML
ChainResidueDetails
AARG36-LEU48

site_idPS00751
Number of Residues17
DetailsTCP1_2 Chaperonins TCP-1 signature 2. VTNDGVTILreMsVeHP
ChainResidueDetails
AVAL57-PRO73

site_idPS00995
Number of Residues9
DetailsTCP1_3 Chaperonins TCP-1 signature 3. QEkeVGDGT
ChainResidueDetails
AGLN85-THR93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
DetailsRegion: {"description":"Nucleotide-sensing loop","evidences":[{"source":"PubMed","id":"22193720","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsActive site: {"evidences":[{"source":"PubMed","id":"20573955","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5W74","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5W74","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20573955","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20573955","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5W74","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20573955","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5W74","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22193720","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22193720","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues8
DetailsSite: {"description":"ATP sensor","evidences":[{"source":"PubMed","id":"22193720","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon