1xfw

Crystal structure of anthrax edema factor (EF) in complex with calmodulin and 3'5' cyclic AMP (cAMP)

Method: X-RAY DIFFRACTION

▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

Calmodulin-sensitive adenylate cyclase

Bacillus anthracis

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Calmodulin 2 × 1 （P62158） MAGNESIUM ION × 1 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1 CALCIUM ION × 3 water × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Calmodulin 2 × 1 （P62158） MAGNESIUM ION × 1 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1 CALCIUM ION × 3 water × 1	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Calmodulin 2 × 1 （P62158） MAGNESIUM ION × 1 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1 CALCIUM ION × 3 water × 1	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Calmodulin 2 × 1 （P62158） MAGNESIUM ION × 1 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1 CALCIUM ION × 3 water × 1	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	Calmodulin 2 × 1 （P62158） MAGNESIUM ION × 1 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1 CALCIUM ION × 3 water × 1	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	Calmodulin 2 × 1 （P62158） MAGNESIUM ION × 1 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1 CALCIUM ION × 3 water × 1	Consistent with protein count
7	Protein heterocomplex	Heteromer	Protein 4	Calmodulin 2 × 2 （P62158） MAGNESIUM ION × 2 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 CALCIUM ION × 6 water × 2	Consistent with protein count
8	Protein heterocomplex	Heteromer	Protein 4	Calmodulin 2 × 2 （P62158） MAGNESIUM ION × 2 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 CALCIUM ION × 6 water × 2	Consistent with protein count
9	Protein heterocomplex	Heteromer	Protein 4	Calmodulin 2 × 2 （P62158） MAGNESIUM ION × 2 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 CALCIUM ION × 6 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CYAA_BACAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 10–777； UniProt 33–800 Author chain B； PDBConstruct 10–777； UniProt 33–800 Author chain C； PDBConstruct 10–777； UniProt 33–800 Author chain D； PDBConstruct 10–777； UniProt 33–800 Author chain E； PDBConstruct 10–777； UniProt 33–800 Author chain F； PDBConstruct 10–777； UniProt 33–800

Calmodulin 2

Homo sapiens

UniProt P62158

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Calmodulin-sensitive adenylate cyclase × 1 （P40136） MAGNESIUM ION × 1 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1 CALCIUM ION × 3 water × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Calmodulin-sensitive adenylate cyclase × 1 （P40136） MAGNESIUM ION × 1 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1 CALCIUM ION × 3 water × 1	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Calmodulin-sensitive adenylate cyclase × 1 （P40136） MAGNESIUM ION × 1 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1 CALCIUM ION × 3 water × 1	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Calmodulin-sensitive adenylate cyclase × 1 （P40136） MAGNESIUM ION × 1 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1 CALCIUM ION × 3 water × 1	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	Calmodulin-sensitive adenylate cyclase × 1 （P40136） MAGNESIUM ION × 1 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1 CALCIUM ION × 3 water × 1	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	Calmodulin-sensitive adenylate cyclase × 1 （P40136） MAGNESIUM ION × 1 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1 CALCIUM ION × 3 water × 1	Consistent with protein count
7	Protein heterocomplex	Heteromer	Protein 4	Calmodulin-sensitive adenylate cyclase × 2 （P40136） MAGNESIUM ION × 2 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 CALCIUM ION × 6 water × 2	Consistent with protein count
8	Protein heterocomplex	Heteromer	Protein 4	Calmodulin-sensitive adenylate cyclase × 2 （P40136） MAGNESIUM ION × 2 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 CALCIUM ION × 6 water × 2	Consistent with protein count
9	Protein heterocomplex	Heteromer	Protein 4	Calmodulin-sensitive adenylate cyclase × 2 （P40136） MAGNESIUM ION × 2 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 CALCIUM ION × 6 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CALM_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain O； PDBConstruct 1–149； UniProt 1–149 Author chain P； PDBConstruct 1–149； UniProt 1–149 Author chain Q； PDBConstruct 1–149； UniProt 1–149 Author chain R； PDBConstruct 1–149； UniProt 1–149 Author chain S； PDBConstruct 1–149； UniProt 1–149 Author chain T； PDBConstruct 1–149； UniProt 1–149

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1xfw
Deposition date deposition_date	2004-09-15
Structure title title	Crystal structure of anthrax edema factor (EF) in complex with calmodulin and 3'5' cyclic AMP (cAMP)
Keywords keywords	protein-protein interaction, LYASE-METAL BINDING PROTEIN COMPLEX; LYASE/METAL BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1xfw__assembly_7__model_1

Assembly 7 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1xfw__assembly_7__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1xfw__assembly_7__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	45.14 Å
Rg (electron density)	44.81 Å
Total Rg	44.98 Å
Atom count	14328
Residues	1762
Excluded volume	255330 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1xfw__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1xfw__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1xfw__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1xfw__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`1xfw__assembly_5__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`1xfw__assembly_6__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`1xfw__assembly_7__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`1xfw__assembly_8__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
9	1	`1xfw__assembly_9__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Calmodulin-sensitive adenylate cyclase
Molecular weight formula_weight	90128.9 kDa
EC 编号 ec_number	4.6.1.1
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	42990

MHHHHHHAAAMNEHYTESDIKRNHKTEKNKTEKEKFKDSINNLVKTEFTNETLDKIQQTQDLLKKIPKDVLEIYSELGGEIYFTDIDLVEHKELQDLSEEEKNSMNSRGEKVPFASRFVFEKKRETPKLIINIKDYAINSEQSKEVYYEIGKGISLDIISKDKSLDPEFLNLIKSLSDDSDSSDLLFSQKFKEKLELNNKSIDINFIKENLTEFQHAFSLAFSYYFAPDHRTVLELYAPDMFEYMNKLEKGGFEKISESLKKEGVEKDRIDVLKGEKALKASGLVPEHADAFKKIARELNTYILFRPVNKLATNLIKSGVATKGLNVHGKSSDWGPVAGYIPFDQDLSKKHGQQLAVEKGNLENKKSITEHEGEIGKIPLKLDHLRIEELKENGIILKGKKEIDNGKKYYLLESNNQVYEFRISDENNEVQYKTKEGKITVLGEKFNWRNIEVMAKNVEGVLKPLTADYDLFALAPSLTEIKKQIPQKEWDKVVNTPNSLEKQKGVTNLLIKYGIERKPDSTKGTLSNWQKQMLDRLNEAVKYTGYTGGDVVNHGTEQDNEEFPEKDNEIFIINPEGEFILTKNWEMTGRFIEKNITGKDYLYYFNRSYNKIAPGNKAYIEWTDPITKAKINTIPTSAEFIKNLSSIRRSSNVGVYKDSGDKDEFAKKESVKKIAGYLSDYYNSANHIFSQEKKRKISIFRGIQAYNEIENVLKSKQIAPEYKNYFQYLKERITNQVQLLLTHQKSNIEFKLLYKQLNFTENETDNFEVFQKIIDEK

Source Source

Source organism organism	Bacillus anthracis
NCBI taxonomy ID ncbi_taxonomy_id	1392
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Calmodulin 2
Molecular weight formula_weight	16851.6 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	O,P,Q,R,S,T

MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDQMIREADIDGDGQVNYEEFVQMMTAK

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 4 Entity 4 non-polymer

Description description	ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE
Molecular weight formula_weight	329.2 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 5 Entity 5 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	18

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	6

▼

6. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1xfwo1
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.5 — Calmodulin-like

Domain ID domain_id	d1xfwp1
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.5 — Calmodulin-like

Domain ID domain_id	d1xfwq1
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.5 — Calmodulin-like

Domain ID domain_id	d1xfwr1
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.5 — Calmodulin-like

Domain ID domain_id	d1xfws1
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.5 — Calmodulin-like

Domain ID domain_id	d1xfwt1
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.5 — Calmodulin-like

CATH v4.4 (30 domains)

Domain ID domain_id	1xfwA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily	10 — Collagenase (Catalytic Domain)

Domain ID domain_id	1xfwA03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1760 — Adenylylcyclase toxin fold
Homologous superfamily homologous superfamily	10 — Anthrax toxin, edema factor, central domain

Domain ID domain_id	1xfwA04
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	1xfwB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily	10 — Collagenase (Catalytic Domain)

Domain ID domain_id	1xfwB03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1760 — Adenylylcyclase toxin fold
Homologous superfamily homologous superfamily	10 — Anthrax toxin, edema factor, central domain

Domain ID domain_id	1xfwB04
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	1xfwC01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily	10 — Collagenase (Catalytic Domain)

Domain ID domain_id	1xfwC03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1760 — Adenylylcyclase toxin fold
Homologous superfamily homologous superfamily	10 — Anthrax toxin, edema factor, central domain

Domain ID domain_id	1xfwC04
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	1xfwD01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily	10 — Collagenase (Catalytic Domain)

Domain ID domain_id	1xfwD03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1760 — Adenylylcyclase toxin fold
Homologous superfamily homologous superfamily	10 — Anthrax toxin, edema factor, central domain

Domain ID domain_id	1xfwD04
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	1xfwE01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily	10 — Collagenase (Catalytic Domain)

Domain ID domain_id	1xfwE03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1760 — Adenylylcyclase toxin fold
Homologous superfamily homologous superfamily	10 — Anthrax toxin, edema factor, central domain

Domain ID domain_id	1xfwE04
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	1xfwF01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily	10 — Collagenase (Catalytic Domain)

Domain ID domain_id	1xfwF03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1760 — Adenylylcyclase toxin fold
Homologous superfamily homologous superfamily	10 — Anthrax toxin, edema factor, central domain

Domain ID domain_id	1xfwF04
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	1xfwO01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1xfwO02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1xfwP01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1xfwP02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1xfwQ01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1xfwQ02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1xfwR01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1xfwR02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1xfwS01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1xfwS02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1xfwT01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1xfwT02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

▶

Unit-cell length a length_a	320.501 Å
Unit-cell length b length_b	185.044 Å
Unit-cell length c length_c	142.454 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.22 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	24

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	3.400 Å
Low-resolution limit resolution_low	29.680 Å
R factor r_factor	0.2660
R_work r_work	0.2660
R_free r_free	0.2830

Crystal structure of anthrax edema factor (EF) in complex with calmodulin and 3'5' cyclic AMP (cAMP)

1. Protein Identity and Related Structures Protein Identity & Related Structures

Calmodulin-sensitive adenylate cyclase

State in the Current Structure

Other States of the Same Protein in the Database

Calmodulin 2

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1xfw__assembly_7__model_1

1xfw__assembly_7__model_1 | I(q)

1xfw__assembly_7__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (6 domains)

CATH v4.4 (30 domains)

7. Citations (1)

Crystal structure of anthrax edema factor (EF) in complex with calmodulin and 3'5' cyclic AMP (cAMP)

1. Protein Identity and Related Structures Protein Identity & Related Structures

Calmodulin-sensitive adenylate cyclase

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Calmodulin 2

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1xfw__assembly_7__model_1

1xfw__assembly_7__model_1 | I(q)

1xfw__assembly_7__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (6 domains)

CATH v4.4 (30 domains)

7. Citations (1)