5ZMW: E309Q mutant of SR Ca2+-ATPase in E2(TG)

Crystal structure of the E309Q mutant of SR Ca2+-ATPase in E2(TG). Determined by X-ray diffraction at 2.5 Å resolution. Released 3 Apr 2019.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Oryctolagus cuniculus
Chains: 1
Atoms: 8,068
Mol. weight: 111.91 kDa
Ligands: DMU, TG1
Released: 3 Apr 2019

Explore 5ZMW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5ZMW contains 59 α-helices and 37 β-strands across 1 chain. 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: 59 helices, 37 β-strands

Element	Residues	Length	Sheet
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	47-49	3
α-helix	51-75	25
α-helix	86-88	3
α-helix	90-122	33
β-strand	126-130	5	3
β-strand	131	1	2
β-strand	138-141	4	3
α-helix	142-144	3
β-strand	150-153	4	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
α-helix	178-181	4
β-strand	187-188	2	4
α-helix	193-194	2
β-strand	207-208	2	3
β-strand	213-216	4	4
β-strand	219-225	7	3
α-helix	227-229	3
α-helix	231-234	4
α-helix	240-242	3
α-helix	248-274	27
α-helix	276-280	5
α-helix	287-293	7
α-helix	295-306	12
α-helix	311-328	18
β-strand	331-333	3	5
α-helix	336-342	7
β-strand	347-351	5	5
α-helix	352-356	5
β-strand	357	1	6
β-strand	362-373	12	7
β-strand	376-384	9	7
β-strand	395-396	2	7
β-strand	401	1	7
α-helix	404-406	3
α-helix	408-419	12
β-strand	424-428	5	8
β-strand	433-437	5	8
α-helix	440-452	13
α-helix	464-468	5
α-helix	470-478	9
β-strand	479-488	10	7
β-strand	493-500	8	7
α-helix	506-508	3
β-strand	511-516	6	7
α-helix	518-521	4
α-helix	522-524	3
β-strand	525-530	6	7
β-strand	533-536	4	7
α-helix	539-554	16
β-strand	560-567	8	7
α-helix	581-583	3
α-helix	584-587	4
β-strand	591-600	10	7
α-helix	602	1
β-strand	603	1	6
α-helix	604	1
α-helix	607-616	10
β-strand	620-625	6	5
α-helix	629-639	11
β-strand	652-654	3	5
α-helix	655-660	6
α-helix	663-670	8
β-strand	675-677	3	5
α-helix	681-693	13
β-strand	698-702	5	5
α-helix	705-707	3
α-helix	708-713	6
β-strand	716-720	5	5
α-helix	725-729	5
β-strand	733-735	3	5
α-helix	740-780	41
α-helix	789-794	6
α-helix	795-799	5
α-helix	801-807	7
α-helix	810-813	4
α-helix	820-823	4
α-helix	832-857	26
α-helix	867-870	4
α-helix	873-875	3
α-helix	881-883	3
α-helix	888-892	5
α-helix	894-914	21
α-helix	927-929	3
α-helix	931-949	19
α-helix	954-957	4
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	protein	1000	Oryctolagus cuniculus	P04191 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5ZMW_1 Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (chains A)
SDNAIAMEAAHSKSTEECLAYFGVSETTGLTPDQVKRHLEKYGHNELPAEEGKSLWELVI
EQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILIANAIVGVWQERNAEN
AIEALKEYEPEMGKVYRADRKSVQRIKARDIVPGDIVEVAVGDKVPADIRILSIKSTTLR
VDQSILTGESVSVIKHTEPVPDPRAVNQDKKNMLFSGTNIAAGKALGIVATTGVSTEIGK
IRDQMAATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWIRGAIY
YFKIAVALAVAAIPQGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTG
TLTTNQMSVCKMFIIDKVDGDFCSLNEFSITGSTYAPEGEVLKNDKPIRSGQFDGLVELA
TICALCNDSSLDFNETKGVYEKVGEATETALTTLVEKMNVFNTEVRNLSKVERANACNSV
IRQLMKKEFTLEFSRDRKSMSVYCSPAKSSRAAVGNKMFVKGAPEGVIDRCNYVRVGTTR
VPMTGPVKEKILSVIKEWGTGRDTLRCLALATRDTPPKREEMVLDDSSRFMEYETDLTFV
GVVGMLDPPRKEVMGSIQLCRDAGIRVIMITGDNKGTAIAICRRIGIFGENEEVADRAYT
GREFDDLPLAEQREACRRACCFARVEPSHKSKIVEYLQSYDEITAMTGDGVNDAPALKKA
EIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVC
IFLTAALGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRPPRSPKEPLISGWLF
FRYMAIGGYVGAATVGAAAWWFMYAEDGPGVTYHQLTHFMQCTEDHPHFEGLDCEIFEAP
EPMTMALSVLVTIEMCNALNSLSENQSLMRMPPWVNIWLLGSICLSMSLHFLILYVDPLP
MIFKLKALDLTQWLMVLKISLPVIGLDEILKFIARNYLEG

Ligands and cofactors

ID	Name	Formula	Copies
DMU	Decyl-beta-D-maltopyranoside	C22 H42 O11	2
TG1	Octanoic acid [3S-[3ALPHA, 3ABETA, 4ALPHA, 6BETA, 6ABETA, 7BETA, 8ALPHA(Z),…	C34 H50 O12	1

Water and common crystallization additives (SO4, NA) are not listed.

Primary citation

Mechanism of the E2 to E1 transition in Ca2+pump revealed by crystal structures of gating residue mutants. Tsunekawa, N., Ogawa, H., Tsueda, J. et al. Proc Natl Acad Sci U S A (2018) 115:12722-12727. DOI 10.1073/pnas.1815472115 · 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

Browse structure collections

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