Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3KFB

Crystal structure of a group II chaperonin from Methanococcus maripaludis

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	21
Details	BINDING SITE FOR RESIDUE ANP A 544

Chain	Residue
A	THR38
A	THR94
A	THR95
A	GLY160
A	LYS161
A	ASP386
A	GLY403
A	GLY404
A	LEU473
A	ASN474
A	PHE476
A	LEU39
A	GLU490
A	MG545
A	GLY40
A	PRO41
A	ASN59
A	ASP60
A	GLY61
A	ASP91
A	THR93

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 545

Chain	Residue
A	ASP91
A	SER157
A	ANP544

site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ANP B 544

Chain	Residue
B	THR38
B	LEU39
B	GLY40
B	PRO41
B	ASN59
B	ASP60
B	GLY61
B	ASP91
B	THR93
B	THR94
B	THR95
B	GLY160
B	LYS161
B	ASP386
B	GLY403
B	GLY404
B	LEU473
B	ASN474
B	PHE476
B	GLU490
B	MG545

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 545

Chain	Residue
B	ASP91
B	SER157
B	ANP544

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ANP C 544

Chain	Residue
C	THR38
C	LEU39
C	GLY40
C	PRO41
C	ASN59
C	ASP60
C	GLY61
C	ASP91
C	THR93
C	THR94
C	THR95
C	GLY160
C	LYS161
C	ASP386
C	GLY403
C	GLY404
C	LEU473
C	ASN474
C	PHE476
C	GLU490
C	MG545

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 545

Chain	Residue
C	ASP91
C	SER157
C	ANP544

site_id	AC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ANP D 544

Chain	Residue
D	THR38
D	LEU39
D	GLY40
D	PRO41
D	ASN59
D	ASP60
D	GLY61
D	ASP91
D	THR93
D	THR94
D	THR95
D	GLY160
D	LYS161
D	ASP386
D	GLY403
D	GLY404
D	LEU473
D	ASN474
D	PHE476
D	GLU490
D	MG545

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 545

Chain	Residue
D	ASP91
D	SER157
D	ANP544

site_id	AC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ANP E 544

Chain	Residue
E	PRO41
E	ASN59
E	ASP60
E	GLY61
E	ASP91
E	THR93
E	THR94
E	THR95
E	GLY160
E	LYS161
E	ASP386
E	GLY403
E	GLY404
E	LEU473
E	ASN474
E	PHE476
E	GLU490
E	MG545
E	THR38
E	LEU39
E	GLY40

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG E 545

Chain	Residue
E	ASP91
E	SER157
E	ANP544

site_id	BC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ANP F 544

Chain	Residue
F	THR38
F	LEU39
F	GLY40
F	PRO41
F	ASN59
F	ASP60
F	GLY61
F	ASP91
F	THR93
F	THR94
F	THR95
F	GLY160
F	LYS161
F	ASP386
F	GLY403
F	GLY404
F	LEU473
F	ASN474
F	PHE476
F	GLU490
F	MG545

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 545

Chain	Residue
F	ASP91
F	SER157
F	LYS161
F	ASP386
F	ANP544

site_id	BC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ANP G 544

Chain	Residue
G	THR38
G	LEU39
G	GLY40
G	PRO41
G	ASN59
G	ASP60
G	GLY61
G	ASP91
G	THR93
G	THR94
G	THR95
G	GLY160
G	LYS161
G	ASP386
G	GLY403
G	GLY404
G	LEU473
G	ASN474
G	PHE476
G	GLU490
G	MG545

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG G 545

Chain	Residue
G	ASP91
G	SER157
G	ANP544

site_id	BC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ANP H 544

Chain	Residue
H	THR38
H	LEU39
H	GLY40
H	PRO41
H	ASN59
H	ASP60
H	GLY61
H	ASP91
H	THR93
H	THR94
H	THR95
H	GLY160
H	LYS161
H	ASP386
H	GLY403
H	GLY404
H	LEU473
H	ASN474
H	PHE476
H	GLU490
H	MG545

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG H 545

Chain	Residue
H	ASP91
H	SER157
H	ANP544

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

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