Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1Q3S

Crystal structure of the chaperonin from Thermococcus strain KS-1 (FormIII crystal complexed with ADP)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0005524	molecular_function	ATP binding
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
C	0005524	molecular_function	ATP binding
C	0006457	biological_process	protein folding
C	0016887	molecular_function	ATP hydrolysis activity
C	0051082	molecular_function	unfolded protein binding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0005524	molecular_function	ATP binding
D	0006457	biological_process	protein folding
D	0016887	molecular_function	ATP hydrolysis activity
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
E	0005524	molecular_function	ATP binding
E	0006457	biological_process	protein folding
E	0016887	molecular_function	ATP hydrolysis activity
E	0051082	molecular_function	unfolded protein binding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
F	0005524	molecular_function	ATP binding
F	0006457	biological_process	protein folding
F	0016887	molecular_function	ATP hydrolysis activity
F	0051082	molecular_function	unfolded protein binding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
G	0005524	molecular_function	ATP binding
G	0006457	biological_process	protein folding
G	0016887	molecular_function	ATP hydrolysis activity
G	0051082	molecular_function	unfolded protein binding
G	0140662	molecular_function	ATP-dependent protein folding chaperone
H	0005524	molecular_function	ATP binding
H	0006457	biological_process	protein folding
H	0016887	molecular_function	ATP hydrolysis activity
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	3
Details	BINDING SITE FOR RESIDUE MG A 1527

Chain	Residue
A	ASP95
A	LYS165
A	ADP1528

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 2527

Chain	Residue
B	ASP95
B	ADP2528

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 3527

Chain	Residue
C	ASP95
C	LYS165
C	ADP3528

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 4527

Chain	Residue
D	LYS165
D	ADP4528
D	ASP95

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG E 5527

Chain	Residue
E	ASP95
E	LYS165
E	ADP5528

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG G 6527

Chain	Residue
G	ASP95
G	ADP7528

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG H 8527

Chain	Residue
H	ASP95
H	LYS165
H	ADP8528

site_id	AC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ADP A 1528

Chain	Residue
A	THR42
A	GLY44
A	PRO45
A	ASN63
A	ASP95
A	GLY96
A	THR97
A	THR98
A	THR99
A	GLY164
A	ALA410
A	GLY411
A	LEU451
A	ILE479
A	ASP480
A	VAL481
A	PHE482
A	GLU496
A	MG1527

site_id	AC9
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ADP B 2528

Chain	Residue
B	THR42
B	LEU43
B	GLY44
B	PRO45
B	ASN63
B	ASP95
B	GLY96
B	THR97
B	THR98
B	THR99
B	GLY164
B	ALA410
B	GLY411
B	LEU451
B	ILE479
B	ASP480
B	VAL481
B	ILE494
B	GLU496
B	MG2527

site_id	BC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP C 3528

Chain	Residue
C	THR42
C	LEU43
C	GLY44
C	PRO45
C	ASN63
C	ASP95
C	GLY96
C	THR97
C	THR98
C	THR99
C	GLY164
C	ALA410
C	GLY411
C	LEU451
C	ILE479
C	ASP480
C	VAL481
C	PHE482
C	GLU496
C	LYS501
C	MG3527

site_id	BC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ADP D 4528

Chain	Residue
D	THR42
D	GLY44
D	PRO45
D	ASN63
D	ASP95
D	GLY96
D	THR97
D	THR98
D	THR99
D	GLY164
D	ALA410
D	GLY411
D	LEU451
D	ILE479
D	ASP480
D	VAL481
D	PHE482
D	ILE494
D	GLU496
D	MG4527

site_id	BC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ADP E 5528

Chain	Residue
E	THR42
E	LEU43
E	GLY44
E	PRO45
E	ASN63
E	ASP95
E	GLY96
E	THR97
E	THR98
E	THR99
E	GLY164
E	ALA410
E	GLY411
E	GLY412
E	ILE447
E	LEU451
E	ILE479
E	ASP480
E	VAL481
E	PHE482
E	ILE494
E	GLU496
E	LYS501
E	MG5527

site_id	BC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ADP F 6528

Chain	Residue
F	THR42
F	LEU43
F	GLY44
F	PRO45
F	ASN63
F	ASP95
F	GLY96
F	THR97
F	THR98
F	THR99
F	GLY164
F	ALA410
F	GLY411
F	LEU451
F	ILE479
F	ASP480
F	VAL481
F	PHE482
F	GLU496
F	LYS501

site_id	BC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ADP G 7528

Chain	Residue
G	THR42
G	LEU43
G	GLY44
G	PRO45
G	ASN63
G	ASP95
G	GLY96
G	THR97
G	THR98
G	THR99
G	GLY164
G	ALA410
G	GLY411
G	ILE447
G	LEU451
G	ILE479
G	ASP480
G	VAL481
G	PHE482
G	ILE494
G	GLU496
G	MG6527

site_id	BC6
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ADP H 8528

Chain	Residue
H	THR42
H	LEU43
H	GLY44
H	PRO45
H	ASN63
H	ASP95
H	GLY96
H	THR97
H	THR98
H	THR99
H	GLY164
H	ALA410
H	GLY411
H	ILE447
H	LEU451
H	ILE479
H	ASP480
H	VAL481
H	PHE482
H	ILE494
H	GLU496
H	MG8527

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG40-LEU52

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

Chain	Residue	Details
A	GLN89-THR97

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"14729342","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	56
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14729342","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q3S","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14729342","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q3Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q3S","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"PDB","id":"1Q3S","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
A	THR98
A	THR97
A	ASP64
A	ASP393

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
B	THR98
B	THR97
B	ASP64
B	ASP393

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
C	THR98
C	THR97
C	ASP64
C	ASP393

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
D	THR98
D	THR97
D	ASP64
D	ASP393

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
E	THR98
E	THR97
E	ASP64
E	ASP393

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
F	THR98
F	THR97
F	ASP64
F	ASP393

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
G	THR98
G	THR97
G	ASP64
G	ASP393

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
H	THR98
H	THR97
H	ASP64
H	ASP393

site_id	MCSA1
Number of Residues	4
Details	M-CSA 179

Chain	Residue	Details
A	ASP64	electrostatic stabiliser, hydrogen bond acceptor
A	THR97	electrostatic stabiliser, hydrogen bond donor
A	THR98	electrostatic stabiliser, hydrogen bond donor
A	ASP393	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	4
Details	M-CSA 179

Chain	Residue	Details
B	ASP64	electrostatic stabiliser, hydrogen bond acceptor
B	THR97	electrostatic stabiliser, hydrogen bond donor
B	THR98	electrostatic stabiliser, hydrogen bond donor
B	ASP393	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	4
Details	M-CSA 179

Chain	Residue	Details
C	ASP64	electrostatic stabiliser, hydrogen bond acceptor
C	THR97	electrostatic stabiliser, hydrogen bond donor
C	THR98	electrostatic stabiliser, hydrogen bond donor
C	ASP393	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA4
Number of Residues	4
Details	M-CSA 179

Chain	Residue	Details
D	ASP64	electrostatic stabiliser, hydrogen bond acceptor
D	THR97	electrostatic stabiliser, hydrogen bond donor
D	THR98	electrostatic stabiliser, hydrogen bond donor
D	ASP393	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA5
Number of Residues	4
Details	M-CSA 179

Chain	Residue	Details
E	ASP64	electrostatic stabiliser, hydrogen bond acceptor
E	THR97	electrostatic stabiliser, hydrogen bond donor
E	THR98	electrostatic stabiliser, hydrogen bond donor
E	ASP393	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA6
Number of Residues	4
Details	M-CSA 179

Chain	Residue	Details
F	ASP64	electrostatic stabiliser, hydrogen bond acceptor
F	THR97	electrostatic stabiliser, hydrogen bond donor
F	THR98	electrostatic stabiliser, hydrogen bond donor
F	ASP393	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA7
Number of Residues	4
Details	M-CSA 179

Chain	Residue	Details
G	ASP64	electrostatic stabiliser, hydrogen bond acceptor
G	THR97	electrostatic stabiliser, hydrogen bond donor
G	THR98	electrostatic stabiliser, hydrogen bond donor
G	ASP393	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA8
Number of Residues	4
Details	M-CSA 179

Chain	Residue	Details
H	ASP64	electrostatic stabiliser, hydrogen bond acceptor
H	THR97	electrostatic stabiliser, hydrogen bond donor
H	THR98	electrostatic stabiliser, hydrogen bond donor
H	ASP393	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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