1XFU: Calmodulin-sensitive adenylate cyclase

Crystal structure of anthrax edema factor (EF) truncation mutant, EF-delta 64 in complex with calmodulin. Determined by X-ray diffraction at 3.35 Å resolution. Released 3 May 2005.

Method: X-ray diffraction
Resolution: 3.35 Å
Organisms: Bacillus anthracis, Homo sapiens
Chains: 12
Atoms: 42,852
Mol. weight: 620.54 kDa
Ligands: CA, MG
Released: 3 May 2005

Explore 1XFU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1XFU contains 253 α-helices and 174 β-strands across 12 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A and D: 34 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	67-69	3	1
α-helix	79-86	8
α-helix	91-97	7
β-strand	103-107	5	1
α-helix	137-139	3
β-strand	142-144	3	1
β-strand	151-155	5	1
α-helix	170-176	7
α-helix	180-182	3
α-helix	192-197	6
α-helix	238-249	12
α-helix	256-259	4
α-helix	264-270	7
α-helix	271-275	5
α-helix	276-282	7
α-helix	285-288	4
α-helix	298-300	3
α-helix	309-322	14
β-strand	324-328	5	2
α-helix	330-332	3
α-helix	333-340	8
β-strand	344-345	2	3
β-strand	365	1	4
α-helix	368-370	3
α-helix	379-393	15
β-strand	398-402	5	4
α-helix	407-412	6
β-strand	420-427	8	5
β-strand	430-436	7	5
β-strand	442-447	6	5
β-strand	454-457	4	5
β-strand	472-473	2	5
β-strand	475-479	5	4
β-strand	486-487	2	4
β-strand	488-489	2	3
β-strand	494-499	6	2
β-strand	500	1	6
α-helix	501-505	5
α-helix	510-517	8
α-helix	522-533	12
α-helix	534-538	5
β-strand	541-543	3	7
β-strand	547-549	3	7
α-helix	552-563	12
β-strand	594-596	3	2
β-strand	602-604	3	2
α-helix	608-618	11
α-helix	620-622	3
β-strand	624	1	6
β-strand	632	1	8
β-strand	643	1	8
α-helix	648-651	4
α-helix	660-671	12
α-helix	685-704	20
α-helix	707-711	5
α-helix	714-736	23
α-helix	743-764	22
α-helix	773-778	6
α-helix	787-796	10

Chains B, C and F: 34 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	67-69	3	9
α-helix	79-86	8
α-helix	91-97	7
β-strand	103-107	5	9
α-helix	137-139	3
β-strand	142-144	3	9
β-strand	151-155	5	9
α-helix	170-176	7
α-helix	180-182	3
α-helix	192-197	6
α-helix	238-249	12
α-helix	256-259	4
α-helix	264-270	7
α-helix	271-275	5
α-helix	276-282	7
α-helix	285-288	4
α-helix	298-300	3
α-helix	309-322	14
β-strand	324-328	5	10
α-helix	330-332	3
α-helix	333-340	8
β-strand	344-345	2	11
β-strand	365	1	12
α-helix	368-370	3
α-helix	379-393	15
β-strand	398-402	5	12
α-helix	407-412	6
β-strand	420-427	8	13
β-strand	430-436	7	13
β-strand	442-447	6	13
β-strand	454-457	4	13
β-strand	472-473	2	13
β-strand	475-479	5	12
β-strand	486-487	2	12
β-strand	488-489	2	11
β-strand	494-499	6	10
β-strand	500	1	14
α-helix	501-505	5
α-helix	510-517	8
α-helix	522-533	12
α-helix	534-538	5
β-strand	541-543	3	15
β-strand	547-549	3	15
α-helix	551-563	13
β-strand	594-596	3	10
β-strand	602-604	3	10
α-helix	608-618	11
α-helix	620-622	3
β-strand	624	1	14
β-strand	632	1	16
β-strand	643	1	16
α-helix	648-651	4
α-helix	660-671	12
α-helix	685-704	20
α-helix	707-711	5
α-helix	714-736	23
α-helix	743-764	22
α-helix	773-778	6
α-helix	787-796	10

Chain E: 34 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	67-69	3	33
α-helix	79-86	8
α-helix	91-97	7
β-strand	103-107	5	33
α-helix	137-139	3
β-strand	142-144	3	33
β-strand	151-155	5	33
α-helix	170-176	7
α-helix	180-182	3
α-helix	192-197	6
α-helix	238-249	12
α-helix	256-259	4
α-helix	264-270	7
α-helix	271-275	5
α-helix	276-279	4
α-helix	285-288	4
α-helix	298-300	3
α-helix	309-322	14
β-strand	324-328	5	34
α-helix	330-332	3
α-helix	333-340	8
β-strand	344-345	2	35
β-strand	365	1	36
α-helix	368-370	3
α-helix	379-393	15
β-strand	398-402	5	36
α-helix	407-412	6
β-strand	420-426	7	37
β-strand	431-436	6	37
β-strand	442-447	6	37
β-strand	454-457	4	37
β-strand	472-473	2	37
β-strand	475-479	5	36
β-strand	486-487	2	36
β-strand	488-489	2	35
β-strand	494-499	6	34
β-strand	500	1	38
α-helix	501-505	5
α-helix	510-517	8
α-helix	522-533	12
α-helix	534-538	5
β-strand	541-543	3	39
β-strand	547-549	3	39
α-helix	551-563	13
β-strand	594-596	3	34
β-strand	602-604	3	34
α-helix	608-618	11
α-helix	620-622	3
β-strand	624	1	38
β-strand	632	1	40
β-strand	643	1	40
α-helix	648-651	4
α-helix	660-671	12
α-helix	685-704	20
α-helix	707-711	5
α-helix	714-736	23
α-helix	743-764	22
α-helix	773-778	6
α-helix	787-796	10

Chains O, P, Q, R and T: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	7-14	8
β-strand	26-27	2	49
α-helix	29-38	10
α-helix	47-52	6
β-strand	63-64	2	49
α-helix	65-71	7
α-helix	84-92	9
β-strand	99-100	2	50
α-helix	102-111	10
α-helix	118-128	11
β-strand	136-137	2	50
α-helix	138-146	9

Chain S: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	7-14	8
β-strand	26-27	2	57
α-helix	29-38	10
α-helix	47-52	6
β-strand	63-64	2	57
α-helix	65-71	7
α-helix	81-83	3
α-helix	84-92	9
β-strand	99-100	2	58
α-helix	102-111	10
α-helix	118-128	11
β-strand	136-137	2	58
α-helix	138-146	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calmodulin-sensitive adenylate cyclase	A, B, C, D, E, F	protein	747	Bacillus anthracis	P40136 (AlphaFold model)
Calmodulin 2	O, P, Q, R, S, T	protein	149	Homo sapiens	P0DP23 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>1XFU_1 Calmodulin-sensitive adenylate cyclase (chains A, B, C, D, E, F)
MHHHHHHAAANNLVKTEFTNETLDKIQQTQDLLKKIPKDVLEIYSELGGEIYFTDIDLVE
HKELQDLSEEEKNSMNSRGEKVPFASRFVFEKKRETPKLIINIKDYAINSEQSKEVYYEI
GKGISLDIISKDKSLDPEFLNLIKSLSDDSDSSDLLFSQKFKEKLELNNKSIDINFIKEN
LTEFQHAFSLAFSYYFAPDHRTVLELYAPDMFEYMNKLEKGGFEKISESLKKEGVEKDRI
DVLKGEKALKASGLVPEHADAFKKIARELNTYILFRPVNKLATNLIKSGVATKGLNVHGK
SSDWGPVAGYIPFDQDLSKKHGQQLAVEKGNLENKKSITEHEGEIGKIPLKLDHLRIEEL
KENGIILKGKKEIDNGKKYYLLESNNQVYEFRISDENNEVQYKTKEGKITVLGEKFNWRN
IEVMAKNVEGVLKPLTADYDLFALAPSLTEIKKQIPQKEWDKVVNTPNSLEKQKGVTNLL
IKYGIERKPDSTKGTLSNWQKQMLDRLNEAVKYTGYTGGDVVNHGTEQDNEEFPEKDNEI
FIINPEGEFILTKNWEMTGRFIEKNITGKDYLYYFNRSYNKIAPGNKAYIEWTDPITKAK
INTIPTSAEFIKNLSSIRRSSNVGVYKDSGDKDEFAKKESVKKIAGYLSDYYNSANHIFS
QEKKRKISIFRGIQAYNEIENVLKSKQIAPEYKNYFQYLKERITNQVQLLLTHQKSNIEF
KLLYKQLNFTENETDNFEVFQKIIDEK

Sequence of entity 2 (O, P, Q, R, S, T), FASTA

>1XFU_2 Calmodulin 2 (chains O, P, Q, R, S, T)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDQMIREADIDGDGQVNYEEFVQMMTAK

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	18
MG	Magnesium ion	Mg	6

Primary citation

Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor. Shen, Y., Zhukovskaya, N.L., Guo, Q. et al. EMBO J (2005) 24:929-941. DOI 10.1038/sj.emboj.7600574 · PubMed

Other PDB entries of the same protein (UniProt P40136 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1K8T 2.6 Å, Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF)
1K90 2.75 Å, Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex…
1K93 2.95 Å, Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex…
1S26 3.0 Å, Structure of Anthrax Edema Factor-Calmodulin-alpha,beta-methyleneadenosine…
1SK6 3.2 Å, Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex…
1XFX 3.2 Å, Crystal structure of anthrax edema factor (EF) in complex with calmodulin in the…
6UZB 3.2 Å, Anthrax toxin protective antigen channels bound to edema factor
1XFZ 3.25 Å, Crystal structure of anthrax edema factor (EF) in complex with calmodulin in the…
1PK0 3.3 Å, Crystal Structure of the EF3-CaM complexed with PMEApp
1XFY 3.3 Å, Crystal structure of anthrax edema factor (EF) in complex with calmodulin
6VRA 3.3 Å, Anthrax octamer prechannel bound to full-length edema factor
1XFV 3.35 Å, Crystal structure of anthrax edema factor (EF) in complex with calmodulin and 3' deoxy-ATP

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