3FGO: PDB entry 3FGO

Crystal Structure of the E2 magnesium fluoride complex of the (SR) Ca2+-ATPase with bound CPA and AMPPCP. Determined by X-ray diffraction at 2.5 Å resolution. Released 7 Apr 2009.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Oryctolagus cuniculus
Chains: 2
Atoms: 15,950
Mol. weight: 221.62 kDa
Ligands: MF4, CZA, ACP, MN
Released: 7 Apr 2009

Explore 3FGO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3FGO contains 121 α-helices and 66 β-strands across 2 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.

Chain A: 60 helices, 33 β-strands

Element	Residues	Length	Sheet
α-helix	9-16	8
α-helix	26-36	11
α-helix	41-43	3
α-helix	49-56	8
α-helix	60-74	15
α-helix	90-109	20
α-helix	115-119	5
α-helix	120-122	3
β-strand	126-130	5	1
β-strand	138-141	4	1
α-helix	142-144	3
β-strand	150-154	5	1
α-helix	157	1
β-strand	158	1	2
α-helix	159	1
β-strand	162-168	7	1
β-strand	174-176	3	2
α-helix	178-181	4
α-helix	186	1
β-strand	187-188	2	2
α-helix	189	1
α-helix	201-203	3
β-strand	207-208	2	1
β-strand	213-216	4	2
β-strand	218-225	8	1
α-helix	231-240	10
α-helix	248-275	28
α-helix	277-279	3
α-helix	291-306	16
α-helix	311-328	18
β-strand	331-333	3	3
α-helix	338-341	4
α-helix	342-344	3
β-strand	347-350	4	3
α-helix	352-356	5
β-strand	357	1	4
β-strand	362-373	12	5
β-strand	376-384	9	5
β-strand	395-397	3	5
β-strand	400-401	2	5
α-helix	404-406	3
α-helix	408-419	12
β-strand	424-428	5	6
β-strand	433-437	5	6
α-helix	440-452	13
α-helix	464-467	4
α-helix	470-478	9
β-strand	479-485	7	5
β-strand	493-500	8	5
α-helix	501	1
β-strand	511-516	6	5
α-helix	518-523	6
β-strand	525-530	6	5
β-strand	533-536	4	5
α-helix	539-552	14
β-strand	560-567	8	5
α-helix	570-572	3
α-helix	573-575	3
α-helix	581-583	3
α-helix	584-587	4
β-strand	591-600	10	5
α-helix	602	1
β-strand	603	1	4
α-helix	604	1
α-helix	607-616	10
β-strand	620-624	5	3
α-helix	629-638	10
β-strand	652-654	3	3
α-helix	655-659	5
α-helix	663-672	10
β-strand	675-677	3	3
α-helix	681-692	12
β-strand	698-702	5	3
α-helix	705-707	3
α-helix	708-713	6
β-strand	716-720	5	3
α-helix	725-730	6
β-strand	733-735	3	3
α-helix	741-780	40
α-helix	789-794	6
α-helix	795-799	5
α-helix	801-807	7
α-helix	811-813	3
α-helix	820-823	4
α-helix	832-852	21
α-helix	867-869	3
α-helix	880-882	3
α-helix	890-892	3
α-helix	894-911	18
α-helix	931-948	18
α-helix	953-956	4
α-helix	964-971	8
α-helix	976-986	11

Chain B: 61 helices, 33 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	9-16	8
α-helix	26-36	11
α-helix	41-43	3
α-helix	49-58	10
α-helix	60-77	18
α-helix	89-107	19
α-helix	115-120	6
β-strand	126-130	5	7
β-strand	138-141	4	7
α-helix	142-144	3
β-strand	150-154	5	7
α-helix	157	1
β-strand	158	1	8
α-helix	159	1
β-strand	162-168	7	7
β-strand	174-176	3	8
α-helix	178-181	4
α-helix	186	1
β-strand	187-188	2	8
α-helix	201-203	3
β-strand	207-208	2	7
β-strand	213-216	4	8
β-strand	218-225	8	7
α-helix	227-229	3
α-helix	231-240	10
α-helix	248-275	28
α-helix	292-306	15
α-helix	311-328	18
β-strand	331-333	3	9
α-helix	338-341	4
α-helix	342-344	3
β-strand	347-350	4	9
α-helix	352-356	5
β-strand	357	1	10
β-strand	362-373	12	11
β-strand	376-384	9	11
β-strand	395-397	3	11
β-strand	400-401	2	11
α-helix	404-406	3
α-helix	408-419	12
β-strand	424-428	5	12
β-strand	433-437	5	12
α-helix	440-452	13
α-helix	464-467	4
α-helix	470-478	9
β-strand	479-485	7	11
β-strand	493-500	8	11
α-helix	503-508	6
β-strand	511-516	6	11
α-helix	518-523	6
β-strand	525-530	6	11
β-strand	533-536	4	11
α-helix	539-552	14
α-helix	559	1
β-strand	560-567	8	11
α-helix	570-572	3
α-helix	573-575	3
α-helix	581-583	3
α-helix	584-587	4
β-strand	591-600	10	11
α-helix	602	1
β-strand	603	1	10
α-helix	604	1
α-helix	607-616	10
β-strand	620-624	5	9
α-helix	629-638	10
β-strand	652-654	3	9
α-helix	655-659	5
α-helix	663-672	10
β-strand	675-677	3	9
α-helix	681-692	12
β-strand	698-702	5	9
α-helix	705-707	3
α-helix	708-713	6
β-strand	716-720	5	9
α-helix	725-729	5
β-strand	733-735	3	9
α-helix	741-781	41
α-helix	783-785	3
α-helix	789-794	6
α-helix	795-799	5
α-helix	801-807	7
α-helix	811-813	3
α-helix	816-818	3
α-helix	820-823	4
α-helix	831-856	26
α-helix	870-876	7
α-helix	890-892	3
α-helix	894-914	21
α-helix	931-947	17
α-helix	952-957	6
α-helix	964-974	11
α-helix	976-985	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Sarcoplasmic/endoplasmic reticulum calcium ATPase 1	A, B	protein	994	Oryctolagus cuniculus	P04191 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3FGO_1 Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (chains A, B)
MEAAHSKSTEECLAYFGVSETTGLTPDQVKRHLEKYGHNELPAEEGKSLWELVIEQFEDL
LVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILIANAIVGVWQERNAENAIEALK
EYEPEMGKVYRADRKSVQRIKARDIVPGDIVEVAVGDKVPADIRILSIKSTTLRVDQSIL
TGESVSVIKHTEPVPDPRAVNQDKKNMLFSGTNIAAGKALGIVATTGVSTEIGKIRDQMA
ATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWIRGAIYYFKIAV
ALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQ
MSVCKMFIIDKVDGDFCSLNEFSITGSTYAPEGEVLKNDKPIRSGQFDGLVELATICALC
NDSSLDFNETKGVYEKVGEATETALTTLVEKMNVFNTEVRNLSKVERANACNSVIRQLMK
KEFTLEFSRDRKSMSVYCSPAKSSRAAVGNKMFVKGAPEGVIDRCNYVRVGTTRVPMTGP
VKEKILSVIKEWGTGRDTLRCLALATRDTPPKREEMVLDDSSRFMEYETDLTFVGVVGML
DPPRKEVMGSIQLCRDAGIRVIMITGDNKGTAIAICRRIGIFGENEEVADRAYTGREFDD
LPLAEQREACRRACCFARVEPSHKSKIVEYLQSYDEITAMTGDGVNDAPALKKAEIGIAM
GSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAA
LGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRPPRSPKEPLISGWLFFRYMAI
GGYVGAATVGAAAWWFMYAEDGPGVTYHQLTHFMQCTEDHPHFEGLDCEIFEAPEPMTMA
LSVLVTIEMCNALNSLSENQSLMRMPPWVNIWLLGSICLSMSLHFLILYVDPLPMIFKLK
ALDLTQWLMVLKISLPVIGLDEILKFIARNYLEG

Ligands and cofactors

ID	Name	Formula	Copies
MF4	TETRAFLUOROMAGNESATE(2-)	F4 Mg	2
CZA	(6AR,11AS,11BR)-10-acetyl-9-hydroxy-7,7-dimethyl-2,6,6A,7,11A,11B-hexahydro-11H…	C20 H20 N2 O3	2
ACP	Phosphomethylphosphonic acid adenylate ester	C11 H18 N5 O12 P3	2
MN	Manganese (II) ion	Mn	3
MG	Magnesium ion	Mg	2

Water and common crystallization additives (K, ACT) are not listed.

Primary citation

Cyclopiazonic acid is complexed to a divalent metal ion when bound to the sarcoplasmic reticulum Ca2+-ATPase. Laursen, M., Bublitz, M., Moncoq, K. et al. J Biol Chem (2009). DOI 10.1074/jbc.C900031200 · PubMed

Other PDB entries of the same protein (UniProt P04191 (AlphaFold model), which also has an AlphaFold model), best resolution first:

27RD 2.0 Å, Crystal structure of SR Ca2+-ATPase in E2(TG) with bound IPP
27QZ 2.1 Å, Crystal structure of SR Ca2+-ATPase in E2(TG) with bound B1HQ
27RC 2.1 Å, Crystal structure of SR Ca2+-ATPase in E2(TG) with bound BMP
27QY 2.12 Å, Crystal structure of SR Ca2+-ATPase in E2(TG) with bound AHQ
3AR4 2.15 Å, Calcium pump crystal structure with bound ATP and TG in the absence of Ca2+
3AR7 2.15 Å, Calcium pump crystal structure with bound TNP-ATP and TG in the absence of Ca2+
27RE 2.2 Å, Crystal structure of SR Ca2+-ATPase in E2(TG) with bound MPQ
27RF 2.2 Å, Crystal structure of SR Ca2+-ATPase in E2(TG) with bound PHQ
3AR5 2.2 Å, Calcium pump crystal structure with bound TNP-AMP and TG
3AR6 2.2 Å, Calcium pump crystal structure with bound TNP-ADP and TG in the absence of calcium
3N5K 2.2 Å, Structure Of The (Sr)Ca2+-ATPase E2-AlF4- Form
1WPG 2.3 Å, Crystal structure of the SR CA2+-ATPase with MGF4

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