Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1Y0V

Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005576	cellular_component	extracellular region
A	0008237	molecular_function	metallopeptidase activity
A	0008294	molecular_function	calcium- and calmodulin-responsive adenylate cyclase activity
A	0046872	molecular_function	metal ion binding
B	0003824	molecular_function	catalytic activity
B	0005576	cellular_component	extracellular region
B	0008237	molecular_function	metallopeptidase activity
B	0008294	molecular_function	calcium- and calmodulin-responsive adenylate cyclase activity
B	0046872	molecular_function	metal ion binding
C	0003824	molecular_function	catalytic activity
C	0005576	cellular_component	extracellular region
C	0008237	molecular_function	metallopeptidase activity
C	0008294	molecular_function	calcium- and calmodulin-responsive adenylate cyclase activity
C	0046872	molecular_function	metal ion binding
D	0003824	molecular_function	catalytic activity
D	0005576	cellular_component	extracellular region
D	0008237	molecular_function	metallopeptidase activity
D	0008294	molecular_function	calcium- and calmodulin-responsive adenylate cyclase activity
D	0046872	molecular_function	metal ion binding
E	0003824	molecular_function	catalytic activity
E	0005576	cellular_component	extracellular region
E	0008237	molecular_function	metallopeptidase activity
E	0008294	molecular_function	calcium- and calmodulin-responsive adenylate cyclase activity
E	0046872	molecular_function	metal ion binding
F	0003824	molecular_function	catalytic activity
F	0005576	cellular_component	extracellular region
F	0008237	molecular_function	metallopeptidase activity
F	0008294	molecular_function	calcium- and calmodulin-responsive adenylate cyclase activity
F	0046872	molecular_function	metal ion binding
H	0005102	molecular_function	signaling receptor binding
H	0005509	molecular_function	calcium ion binding
H	0016460	cellular_component	myosin II complex
H	0046872	molecular_function	metal ion binding
I	0005102	molecular_function	signaling receptor binding
I	0005509	molecular_function	calcium ion binding
I	0016460	cellular_component	myosin II complex
I	0046872	molecular_function	metal ion binding
J	0005102	molecular_function	signaling receptor binding
J	0005509	molecular_function	calcium ion binding
J	0016460	cellular_component	myosin II complex
J	0046872	molecular_function	metal ion binding
K	0005102	molecular_function	signaling receptor binding
K	0005509	molecular_function	calcium ion binding
K	0016460	cellular_component	myosin II complex
K	0046872	molecular_function	metal ion binding
L	0005102	molecular_function	signaling receptor binding
L	0005509	molecular_function	calcium ion binding
L	0016460	cellular_component	myosin II complex
L	0046872	molecular_function	metal ion binding
M	0005102	molecular_function	signaling receptor binding
M	0005509	molecular_function	calcium ion binding
M	0016460	cellular_component	myosin II complex
M	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 900

Chain	Residue
A	ASP491
A	ASP493
A	HIS577

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 901

Chain	Residue
B	ASP491
B	ASP493
B	HIS577

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 902

Chain	Residue
C	ASP491
C	ASP493
C	HIS577

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 903

Chain	Residue
D	LYS346
D	ASP491
D	ASP493
D	HIS577

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG E 904

Chain	Residue
E	ASP491
E	ASP493
E	HIS577

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 905

Chain	Residue
F	ASP491
F	ASP493
F	HIS577

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA H 701

Chain	Residue
H	ASP20
H	ASP22
H	ASP24
H	THR26

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA H 801

Chain	Residue
H	ASP129
H	ASP131
H	ASP133
H	GLN135
H	GLU140

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA H 802

Chain	Residue
H	ASP93
H	ASP95
H	ASN97
H	TYR99
H	GLU104

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA I 703

Chain	Residue
I	ASP20
I	ASP22
I	ASP24
I	THR26

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA I 803

Chain	Residue
I	ASP129
I	ASP131
I	ASP133
I	GLN135
I	GLU140

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA I 804

Chain	Residue
I	ASP93
I	ASP95
I	ASN97
I	TYR99
I	GLU104

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA J 705

Chain	Residue
J	ASP20
J	ASP22
J	ASP24
J	THR26

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA J 805

Chain	Residue
J	ASP129
J	ASP131
J	ASP133
J	GLN135
J	GLU140

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA J 806

Chain	Residue
J	ASP93
J	ASP95
J	ASN97
J	TYR99
J	GLU104

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA K 707

Chain	Residue
K	ASP20
K	ASP22
K	ASP24
K	THR26

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA K 807

Chain	Residue
K	ASP129
K	ASP131
K	ASP133
K	GLN135
K	GLU140

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA K 808

Chain	Residue
K	ASP93
K	ASP95
K	ASN97
K	TYR99
K	GLU104

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA L 709

Chain	Residue
L	ASP20
L	ASP22
L	ASP24
L	THR26

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA L 809

Chain	Residue
L	ASP129
L	ASP131
L	ASP133
L	GLN135
L	GLU140

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA L 810

Chain	Residue
L	ASP93
L	ASP95
L	ASN97
L	TYR99
L	GLU104

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA M 711

Chain	Residue
M	ASP20
M	ASP22
M	ASP24
M	THR26

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA M 811

Chain	Residue
M	ASP129
M	ASP131
M	ASP133
M	GLN135
M	GLU140

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA M 812

Chain	Residue
M	ASP95
M	ASN97
M	TYR99
M	GLU104
M	ASP93

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE POP A 901

Chain	Residue
A	LYS346
A	SER354
A	LYS372

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE POP B 902

Chain	Residue
B	LYS346
B	SER354
B	LYS372

site_id	CC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE POP C 903

Chain	Residue
C	LYS346
C	SER354
C	LYS372

site_id	DC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE POP D 904

Chain	Residue
D	LYS346
D	SER354
D	LYS372

site_id	DC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE POP E 905

Chain	Residue
E	LYS346
E	SER354
E	LYS372

site_id	DC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE POP F 906

Chain	Residue
F	LYS346
F	SER354
F	LYS372

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL

Chain	Residue	Details
H	ASP20-LEU32
H	ASP56-PHE68
H	ASP93-LEU105
H	ASP129-PHE141

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	330
Details	Region: {"description":"Catalytic CA1","evidences":[{"source":"PubMed","id":"11807546","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	834
Details	Region: {"description":"Catalytic CB","evidences":[{"source":"PubMed","id":"11807546","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	792
Details	Region: {"description":"Catalytic CA2","evidences":[{"source":"PubMed","id":"11807546","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11807546","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15719022","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XFU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15719022","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XFW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	210
Details	Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	210
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	210
Details	Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	192
Details	Domain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	120
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	6
Details	Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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