5BWK: ATPase GET3

6.0 A Crystal structure of a Get3-Get4-Get5 intermediate complex from S.cerevisiae. Determined by X-ray diffraction at 6.0 Å resolution. Released 14 Oct 2015.

Method: X-ray diffraction
Resolution: 6.0 Å
Organisms: Saccharomyces cerevisiae (strain RM11-1a), Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains: 24
Atoms: 41,907
Mol. weight: 681.29 kDa
Ligands: ZN
Released: 14 Oct 2015

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

Secondary structure: helices and β-sheets

5BWK contains 265 α-helices and 80 β-strands across 24 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, M and N: 14 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	10-13	4
β-strand	20-24	5	1
α-helix	31-45	15
β-strand	51-55	5	1
α-helix	61-66	6
β-strand	75-76	2	1
α-helix	77	1
β-strand	83-87	5	1
α-helix	136-152	17
β-strand	162-166	5	1
α-helix	175-177	3
α-helix	179-193	15
α-helix	213-229	17
β-strand	236-242	7	1
α-helix	246-261	16
β-strand	266-274	9	1
α-helix	286-305	20
β-strand	310-315	6	1
α-helix	316	1
α-helix	324-331	8
α-helix	332-334	3
α-helix	344-350	7

Chains B and C: 14 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	10-13	4
β-strand	20-24	5	2
α-helix	31-45	15
β-strand	51-55	5	2
α-helix	61-66	6
β-strand	75-76	2	2
α-helix	77	1
β-strand	83-87	5	2
α-helix	136-152	17
β-strand	162-166	5	2
α-helix	175-177	3
α-helix	179-193	15
α-helix	213-230	18
β-strand	236-242	7	2
α-helix	246-261	16
β-strand	266-274	9	2
α-helix	286-305	20
β-strand	310-315	6	2
α-helix	316	1
α-helix	324-331	8
α-helix	332-334	3
α-helix	344-350	7

Chains D and O: 14 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	10-13	4
β-strand	20-24	5	3
α-helix	31-45	15
β-strand	51-55	5	3
α-helix	61-66	6
β-strand	75-76	2	3
α-helix	77	1
β-strand	83-87	5	3
α-helix	136-151	16
β-strand	162-166	5	3
α-helix	175-177	3
α-helix	179-193	15
α-helix	213-229	17
β-strand	236-242	7	3
α-helix	246-261	16
β-strand	266-274	9	3
α-helix	286-305	20
β-strand	310-315	6	3
α-helix	316	1
α-helix	324-331	8
α-helix	332-334	3
α-helix	344-350	7

Chains E, S and W: 16 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	10-24	15
α-helix	29-45	17
α-helix	49-65	17
α-helix	69-85	17
α-helix	88-90	3
α-helix	92-103	12
α-helix	112-125	14
α-helix	134-146	13
α-helix	150-158	9
α-helix	162-178	17
α-helix	186-200	15
α-helix	204-221	18
β-strand	226-231	6	4
β-strand	234-239	6	4
α-helix	243-257	15
α-helix	260-269	10
α-helix	271-276	6
α-helix	278-287	10

Chains F, H, J, R, T and V: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	7-20	14
α-helix	44-48	5
α-helix	51-52	2

Chain G: 16 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	10-24	15
α-helix	29-45	17
α-helix	49-65	17
α-helix	69-85	17
α-helix	88-90	3
α-helix	92-104	13
α-helix	112-125	14
α-helix	134-146	13
α-helix	150-158	9
α-helix	162-178	17
α-helix	186-200	15
α-helix	204-222	19
β-strand	226-231	6	5
β-strand	234-239	6	5
α-helix	243-257	15
α-helix	260-269	10
α-helix	271-276	6
α-helix	278-287	10

Chain I: 15 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	10-24	15
α-helix	29-45	17
α-helix	49-65	17
α-helix	69-85	17
α-helix	92-104	13
α-helix	112-125	14
α-helix	134-146	13
α-helix	150-158	9
α-helix	162-178	17
α-helix	186-200	15
α-helix	204-222	19
β-strand	226-231	6	6
β-strand	234-239	6	6
α-helix	243-257	15
α-helix	260-269	10
α-helix	271-276	6
α-helix	278-287	10

Chain K: 16 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	10-25	16
α-helix	29-45	17
α-helix	49-65	17
α-helix	69-85	17
α-helix	88-90	3
α-helix	92-104	13
α-helix	112-125	14
α-helix	134-146	13
α-helix	150-158	9
α-helix	162-178	17
α-helix	186-200	15
α-helix	204-221	18
β-strand	226-231	6	7
β-strand	234-239	6	7
α-helix	243-257	15
α-helix	260-269	10
α-helix	271-276	6
α-helix	278-287	10

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ATPase GET3	A, B, C, D, M, N, O, P	protein	373	Saccharomyces cerevisiae (strain RM11-1a)	Q12154 (AlphaFold model)
Golgi to ER traffic protein 4	E, G, I, K, Q, S, U, W	protein	319	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	Q12125 (AlphaFold model)
Ubiquitin-like protein MDY2	F, H, J, L, R, T, V, X	protein	56	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	Q12285 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, M, N, O, P), FASTA

>5BWK_1 ATPase GET3 (chains A, B, C, D, M, N, O, P)
MGGSHHHHHHGENLYFQSVDDLTVEPNLHSLITSTTHKWIFVGGKGGVGKTTSSCSIAIQ
MALSQPNKQFLLISTDPAHNLSDAFGEKFGKDARKVTGMNNLSCMEIDPSAALKDMNDMA
VSRANNNGSDGQGDDLGSLLQGGALADLTGSIPGIDEALSFMEVMKHIKRQEQGEGETFD
TVIFDTAPTGHTLRFLQLPNTLSKLLEKFGEITNKLGPMLNSFMGAGNVDISGKLNELKA
NVETIRQQFTDPDLTTFVCVCISEFLSLYETERLIQELISYDMDVNSIIVNQLLFAENDQ
EHNCKRCQARWKMQKKYLDQIDELYEDFHVVKMPLCAGEIRGLNNLTKFSQFLNKEYNPI
TDGKVIYELEDKE

Sequence of entity 2 (E, G, I, K, Q, S, U, W), FASTA

>5BWK_2 Golgi to ER traffic protein 4 (chains E, G, I, K, Q, S, U, W)
MGAKLAKTLQRFENKIKAGDYYEAHQTLRTIANRYVRSKSYEHAIELISQGALSFLKAKQ
GGSGTDLIFYLLEVYDLAEVKVDDISVARLVRLIAELDPSEPNLKDVITGMNNWSIKFSE
YKFGDPYLHNTIGSKLLEGDFVYEAERYFMLGTHDSMIKYVDLLWDWLCQVDDIEDSTVA
EFFSRLVFNYLFISNISFAHESKDIFLERFIEKFHPKYEKIDKNGYEIVFFEDYSDLNFL
QLLLITCQTADASYFLNLKNHYLDFSQAYKSELEFLGQEYFNIVAPKQTNFLQDMMSGFL
GGSGENLYFQSLEHHHHHH

Sequence of entity 3 (F, H, J, L, R, T, V, X), FASTA

>5BWK_3 Ubiquitin-like protein MDY2 (chains F, H, J, L, R, T, V, X)
MSTSASGPEHEFVSKFLTLATLTEPKLPKSYTKPLKDVTNLGVPLPTLKYKYKQNR

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4

Primary citation

Mechanism of Assembly of a Substrate Transfer Complex during Tail-anchored Protein Targeting. Gristick, H.B., Rome, M.E., Chartron, J.W. et al. J Biol Chem (2015) 290:30006-30017. DOI 10.1074/jbc.M115.677328 · PubMed

Other PDB entries of the same protein (UniProt Q12154 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2WOJ 1.99 Å, ADP-AlF4 complex of S. cerevisiae GET3
4XTR 2.05 Å, Structure of Get3 bound to the transmembrane domain of Pep12
3ZS9 2.1 Å, S. cerevisiae Get3-ADP-AlF4- complex with a cytosolic Get2 fragment
3H84 2.3 Å, Crystal structure of GET3
4XVU 2.35 Å, Structure of Get3 bound to the transmembrane domain of Nyv1
4XWO 2.75 Å, Structure of Get3 bound to the transmembrane domain of Sec22
3A36 2.8 Å, Structural insight into the membrane insertion of tail-anchored proteins by Get3
5BW8 2.8 Å, 2.8 A crystal structure of a Get3-Get4-Get5 intermediate complex from S.cerevisiae
3A37 3.0 Å, Structural insight into the membrane insertion of tail-anchored proteins by Get3
3B2E 3.0 Å, Crystal structure of S. cerevisiae Get3 in the open conformation in complex with Get1…
3SJA 3.0 Å, Crystal structure of S. cerevisiae Get3 in the open state in complex with Get1 cytosolic…
3ZS8 3.0 Å, S. cerevisiae Get3 complexed with a cytosolic Get1 fragment

Browse structure collections

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