2AGV: SR CA2+-ATPASE with BHQ and TG

Crystal structure of the SR CA2+-ATPASE with BHQ and TG. Determined by X-ray diffraction at 2.4 Å resolution. Released 25 Oct 2005.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Oryctolagus cuniculus
Chains: 2
Atoms: 15,830
Mol. weight: 225.4 kDa
Ligands: PTY, BHQ, TG1
Released: 25 Oct 2005

Explore 2AGV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2AGV contains 122 α-helices and 74 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, 38 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	9-16	8
β-strand	19	1	1
β-strand	23	1	1
β-strand	24	1	2
α-helix	26-36	11
α-helix	41-46	6
α-helix	49-55	7
α-helix	60-77	18
α-helix	84-86	3
α-helix	89-110	22
α-helix	115-119	5
α-helix	120-122	3
β-strand	126-130	5	3
β-strand	131	1	2
β-strand	138-141	4	3
α-helix	142-144	3
β-strand	150-154	5	3
α-helix	157	1
β-strand	158	1	4
α-helix	159	1
β-strand	162-168	7	3
β-strand	174-176	3	4
β-strand	187-188	2	4
α-helix	201-203	3
β-strand	207-208	2	3
β-strand	213-216	4	4
β-strand	218-225	8	3
α-helix	227-229	3
α-helix	231-240	10
α-helix	245-247	3
α-helix	248-273	26
α-helix	276-280	5
β-strand	282	1	5
α-helix	288-306	19
α-helix	311-327	17
β-strand	331-333	3	6
α-helix	338-343	6
β-strand	347-351	5	6
β-strand	357	1	7
β-strand	362-373	12	8
β-strand	376-384	9	8
β-strand	395-397	3	8
β-strand	400-401	2	8
α-helix	404-406	3
α-helix	408-419	12
β-strand	424-428	5	9
β-strand	433-437	5	9
α-helix	440-452	13
α-helix	464-467	4
α-helix	470-475	6
β-strand	479-485	7	8
β-strand	493-500	8	8
β-strand	511-516	6	8
α-helix	518-523	6
β-strand	525-530	6	8
β-strand	533-536	4	8
α-helix	537-538	2
α-helix	539-554	16
α-helix	559	1
β-strand	560-567	8	8
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	8
α-helix	602	1
β-strand	603	1	7
α-helix	604	1
α-helix	607-616	10
β-strand	620-625	6	6
α-helix	629-639	11
β-strand	652-654	3	6
α-helix	655-659	5
α-helix	663-672	10
β-strand	675-677	3	6
α-helix	683-692	10
β-strand	698-702	5	6
α-helix	704-713	10
β-strand	716-720	5	6
α-helix	725-729	5
β-strand	733-735	3	6
α-helix	740-780	41
α-helix	783-785	3
α-helix	789-794	6
α-helix	795-799	5
α-helix	801-806	6
α-helix	807-809	3
α-helix	810-813	4
α-helix	816-818	3
α-helix	820-823	4
α-helix	832-857	26
α-helix	889-892	4
α-helix	894-913	20
α-helix	927-929	3
α-helix	931-949	19
α-helix	952-957	6
α-helix	964-974	11
α-helix	976-990	15

Chain B: 61 helices, 36 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	9-16	8
β-strand	24	1	10
α-helix	26-36	11
α-helix	41-46	6
β-strand	48	1	5
α-helix	49-55	7
α-helix	60-77	18
α-helix	84-86	3
α-helix	89-110	22
α-helix	115-119	5
α-helix	120-122	3
β-strand	126-130	5	11
β-strand	131	1	10
β-strand	138-141	4	11
α-helix	142-144	3
β-strand	150-154	5	11
α-helix	157	1
β-strand	158	1	12
α-helix	159	1
β-strand	162-168	7	11
β-strand	174-176	3	12
β-strand	187-188	2	12
α-helix	201-203	3
β-strand	207-208	2	11
β-strand	213-216	4	12
β-strand	218-225	8	11
α-helix	227-229	3
α-helix	231-240	10
α-helix	245-247	3
α-helix	248-273	26
α-helix	276-280	5
α-helix	288-306	19
α-helix	311-327	17
β-strand	331-333	3	13
α-helix	338-343	6
β-strand	347-351	5	13
β-strand	357	1	14
β-strand	362-373	12	15
β-strand	376-384	9	15
β-strand	395-397	3	15
β-strand	400-401	2	15
α-helix	404-406	3
α-helix	408-419	12
β-strand	424-428	5	16
β-strand	433-437	5	16
α-helix	440-452	13
α-helix	464-467	4
α-helix	470-475	6
β-strand	479-485	7	15
β-strand	493-500	8	15
β-strand	511-516	6	15
α-helix	518-523	6
β-strand	525-530	6	15
β-strand	533-536	4	15
α-helix	537-538	2
α-helix	539-554	16
α-helix	559	1
β-strand	560-567	8	15
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	15
α-helix	602	1
β-strand	603	1	14
α-helix	604	1
α-helix	607-616	10
β-strand	620-625	6	13
α-helix	629-639	11
β-strand	652-654	3	13
α-helix	655-659	5
α-helix	663-672	10
β-strand	675-677	3	13
α-helix	683-692	10
β-strand	698-702	5	13
α-helix	704-713	10
β-strand	716-720	5	13
α-helix	725-729	5
β-strand	733-735	3	13
α-helix	740-780	41
α-helix	783-785	3
α-helix	789-794	6
α-helix	795-799	5
α-helix	801-806	6
α-helix	807-809	3
α-helix	810-813	4
α-helix	816-818	3
α-helix	820-823	4
α-helix	832-857	26
α-helix	889-892	4
α-helix	894-913	20
α-helix	927-929	3
α-helix	931-949	19
α-helix	952-957	6
α-helix	964-974	11
α-helix	976-990	15

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

>2AGV_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
PTY	Phosphatidylethanolamine	C40 H80 N O8 P	6
BHQ	2,5-ditert-butylbenzene-1,4-diol	C14 H22 O2	2
TG1	Octanoic acid [3S-[3ALPHA, 3ABETA, 4ALPHA, 6BETA, 6ABETA, 7BETA, 8ALPHA(Z),…	C34 H50 O12	2

Water and common crystallization additives (NA) are not listed.

Primary citation

Inaugural Article: Structural role of countertransport revealed in Ca2+ pump crystal structure in the absence of Ca2+. Obara, K., Miyashita, N., Xu, C. et al. Proc Natl Acad Sci U S A (2005) 102:14489-14496. DOI 10.1073/pnas.0506222102 · 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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