4BEW: SERCA

SERCA bound to phosphate analogue. Determined by X-ray diffraction at 2.5 Å resolution. Released 19 Feb 2014.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: ORYCTOLAGUS CUNICULUS
Chains: 2
Atoms: 15,950
Mol. weight: 221.69 kDa
Ligands: MG, CZA, MN, ACP
Released: 19 Feb 2014

Explore 4BEW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4BEW contains 125 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: 61 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	60-77	18
α-helix	87-89	3
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	311-327	17
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	894-913	20
α-helix	931-948	18
α-helix	953-956	4
α-helix	965-971	7
α-helix	976-986	11

Chain B: 64 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	49-54	6
α-helix	55-57	3
α-helix	60-77	18
α-helix	89-107	19
α-helix	115-120	6
β-strand	126-131	6	7
β-strand	134-141	8	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	311-327	17
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	479-488	10	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	741-780	40
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	880-882	3
α-helix	890-892	3
α-helix	894-914	21
α-helix	931-947	17
α-helix	952-957	6
α-helix	961-963	3
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

>4BEW_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
ALDLTQWLMVLKISLPVIGLDEILKFIARNYLED

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	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
MN	Manganese (II) ion	Mn	3
ACP	Phosphomethylphosphonic acid adenylate ester	C11 H18 N5 O12 P3	2
MGF	Trifluoromagnesate	F3 Mg	2

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

Primary citation

Serca Bound to Phosphate Analogue. Mattle, D., Drachmann, N.D., Liu, X.Y. et al. To be published.

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

Browse structure collections

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