Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5W79

Crystal Structure of the Group II Chaperonin from Methanococcus Maripaludis, Cysteine-less mutant in the Apo State

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006457	biological_process	protein folding
A	0016787	molecular_function	hydrolase activity
A	0016853	molecular_function	isomerase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0032991	cellular_component	protein-containing complex
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006457	biological_process	protein folding
B	0016787	molecular_function	hydrolase activity
B	0016853	molecular_function	isomerase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0032991	cellular_component	protein-containing complex
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006457	biological_process	protein folding
C	0016787	molecular_function	hydrolase activity
C	0016853	molecular_function	isomerase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0032991	cellular_component	protein-containing complex
C	0051082	molecular_function	unfolded protein binding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0000166	molecular_function	nucleotide binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006457	biological_process	protein folding
D	0016787	molecular_function	hydrolase activity
D	0016853	molecular_function	isomerase activity
D	0016887	molecular_function	ATP hydrolysis activity
D	0032991	cellular_component	protein-containing complex
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
E	0000166	molecular_function	nucleotide binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006457	biological_process	protein folding
E	0016787	molecular_function	hydrolase activity
E	0016853	molecular_function	isomerase activity
E	0016887	molecular_function	ATP hydrolysis activity
E	0032991	cellular_component	protein-containing complex
E	0051082	molecular_function	unfolded protein binding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
F	0000166	molecular_function	nucleotide binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006457	biological_process	protein folding
F	0016787	molecular_function	hydrolase activity
F	0016853	molecular_function	isomerase activity
F	0016887	molecular_function	ATP hydrolysis activity
F	0032991	cellular_component	protein-containing complex
F	0051082	molecular_function	unfolded protein binding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
G	0000166	molecular_function	nucleotide binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0006457	biological_process	protein folding
G	0016787	molecular_function	hydrolase activity
G	0016853	molecular_function	isomerase activity
G	0016887	molecular_function	ATP hydrolysis activity
G	0032991	cellular_component	protein-containing complex
G	0051082	molecular_function	unfolded protein binding
G	0140662	molecular_function	ATP-dependent protein folding chaperone
H	0000166	molecular_function	nucleotide binding
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0006457	biological_process	protein folding
H	0016787	molecular_function	hydrolase activity
H	0016853	molecular_function	isomerase activity
H	0016887	molecular_function	ATP hydrolysis activity
H	0032991	cellular_component	protein-containing complex
H	0051082	molecular_function	unfolded protein binding
H	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue SO4 A 601

Chain	Residue
A	ASP91
A	GLY92
A	THR93
A	THR94
A	THR95

site_id	AC2
Number of Residues	4
Details	binding site for residue SO4 B 601

Chain	Residue
B	LEU39
B	ASP91
B	GLY92
B	THR94

site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 C 601

Chain	Residue
C	ASP91
C	GLY92
C	THR94
C	THR95

site_id	AC4
Number of Residues	4
Details	binding site for residue SO4 D 601

Chain	Residue
D	ASP91
D	GLY92
D	THR94
D	THR95

site_id	AC5
Number of Residues	4
Details	binding site for residue SO4 E 601

Chain	Residue
E	ASP91
E	GLY92
E	THR94
E	THR95

site_id	AC6
Number of Residues	4
Details	binding site for residue SO4 F 601

Chain	Residue
F	ASP91
F	GLY92
F	THR94
F	THR95

site_id	AC7
Number of Residues	4
Details	binding site for residue SO4 G 601

Chain	Residue
G	ASP91
G	GLY92
G	THR94
G	THR95

site_id	AC8
Number of Residues	4
Details	binding site for residue SO4 H 601

Chain	Residue
H	ASP91
H	GLY92
H	THR94
H	THR95

Functional Information from PROSITE/UniProt

site_id	PS00750
Number of Residues	13
Details	TCP1_1 Chaperonins TCP-1 signature 1. RStLGPkGmdKML

Chain	Residue	Details
A	ARG36-LEU48

site_id	PS00751
Number of Residues	17
Details	TCP1_2 Chaperonins TCP-1 signature 2. VTNDGVTILreMsVeHP

Chain	Residue	Details
A	VAL57-PRO73

site_id	PS00995
Number of Residues	9
Details	TCP1_3 Chaperonins TCP-1 signature 3. QEkeVGDGT

Chain	Residue	Details
A	GLN85-THR93

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	72
Details	Region: {"description":"Nucleotide-sensing loop","evidences":[{"source":"PubMed","id":"22193720","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	208
Details	Region: {"description":"Lid region","evidences":[{"source":"PubMed","id":"17460696","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20573955","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Active site: {"evidences":[{"source":"PubMed","id":"20573955","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	16
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20573955","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5W74","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22193720","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	8
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	8
Details	Site: {"description":"ATP sensor","evidences":[{"source":"PubMed","id":"22193720","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)