4XVU: Get3

Structure of Get3 bound to the transmembrane domain of Nyv1. Determined by X-ray diffraction at 2.35 Å resolution. Released 18 Mar 2015.

Method: X-ray diffraction
Resolution: 2.35 Å
Organisms: Saccharomyces cerevisiae (ATCC 204508 / S288c), Homo sapiens, synthetic construct
Chains: 14
Atoms: 23,945
Mol. weight: 359.09 kDa
Ligands: ATP, MG, ZN
Released: 18 Mar 2015

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

Secondary structure: helices and β-sheets

4XVU contains 130 α-helices and 211 β-strands across 14 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: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	2-23	22

Chain A: 17 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	10-13	4
β-strand	20-25	6	1
α-helix	31-45	15
β-strand	51-55	5	1
α-helix	62-66	5
β-strand	75-76	2	1
α-helix	77	1
β-strand	83-87	5	1
α-helix	90-102	13
α-helix	127-130	4
α-helix	136-153	18
β-strand	162-166	5	1
α-helix	167-169	3
α-helix	170-177	8
α-helix	179-189	11
α-helix	216-230	15
β-strand	236-243	8	1
α-helix	246-261	16
β-strand	268-274	7	1
α-helix	286-305	20
β-strand	310-315	6	1
α-helix	316-317	2
α-helix	323-331	9
α-helix	332-334	3
α-helix	343-348	6

Chain B: 15 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	10-13	4
β-strand	20-25	6	2
α-helix	31-45	15
β-strand	51-55	5	2
α-helix	62-66	5
β-strand	75-76	2	2
α-helix	77	1
β-strand	83-87	5	2
α-helix	90-99	10
α-helix	130-132	3
α-helix	136-153	18
β-strand	162-166	5	2
α-helix	167-169	3
α-helix	170-177	8
α-helix	179-189	11
α-helix	212-230	19
β-strand	236-243	8	2
α-helix	246-261	16
β-strand	268-274	7	2
α-helix	286-305	20
β-strand	310-315	6	2
α-helix	316-317	2
α-helix	323-335	13

Chain C: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	3
β-strand	13-15	3	4
β-strand	21-28	8	3
α-helix	32-34	3
β-strand	36-42	7	4
β-strand	48-55	8	4
α-helix	56-58	3
β-strand	60-63	4	4
β-strand	68	1	3
β-strand	71-76	6	3
β-strand	81-86	6	3
α-helix	91-93	3
β-strand	95-103	9	4
β-strand	106-112	7	4
β-strand	116-120	5	4
α-helix	123-125	3
β-strand	126	1	5
α-helix	127-128	2
β-strand	129-133	5	6
β-strand	140-141	2	6
β-strand	144-154	11	6
β-strand	155	1	5
β-strand	160-163	4	7
α-helix	164-166	3
β-strand	172-174	3	6
α-helix	175-177	3
β-strand	178-179	2	6
β-strand	185-194	10	6
α-helix	195-197	3
β-strand	204-209	6	7
α-helix	210-212	3
β-strand	214-219	6	7

Chain D: 7 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	8
β-strand	11-14	4	9
β-strand	20-26	7	8
β-strand	30	1	10
β-strand	32	1	10
β-strand	34-39	6	9
β-strand	46-50	5	9
β-strand	54-55	2	9
α-helix	56	1
β-strand	63-68	6	8
β-strand	71-76	6	8
α-helix	81-83	3
β-strand	86-91	6	9
β-strand	100-101	2	9
β-strand	105-109	5	9
β-strand	114	1	11
α-helix	115-116	2
β-strand	117-121	5	12
α-helix	122-124	3
α-helix	125-130	6
β-strand	132-142	11	12
β-strand	143	1	11
β-strand	148-153	6	13
β-strand	156-157	2	13
β-strand	162-166	5	12
α-helix	167-170	4
β-strand	176-185	10	12
α-helix	186-189	4
β-strand	194-200	7	13
β-strand	208-213	6	13

Chain E: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	14
β-strand	14-15	2	15
β-strand	21-28	8	14
α-helix	32-34	3
β-strand	35-42	8	16
β-strand	48-55	8	16
α-helix	56-58	3
β-strand	60-63	4	16
β-strand	71-76	6	14
α-helix	77-79	3
β-strand	81-86	6	14
β-strand	95-103	9	16
β-strand	106-112	7	16
β-strand	116-118	3	16
β-strand	119-120	2	15
β-strand	126	1	17
α-helix	127-128	2
β-strand	129-133	5	18
α-helix	134-136	3
β-strand	144-154	11	18
β-strand	155	1	17
β-strand	160-163	4	19
α-helix	164-166	3
β-strand	172-174	3	18
α-helix	175-177	3
β-strand	178-179	2	18
β-strand	185-194	10	18
α-helix	195-197	3
β-strand	204-209	6	19
α-helix	210-212	3
β-strand	214-219	6	19

Chain F: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	20
β-strand	11-14	4	21
β-strand	20-26	7	20
β-strand	34-39	6	21
β-strand	46-50	5	21
β-strand	54-55	2	21
α-helix	56	1
β-strand	63-68	6	20
β-strand	71-76	6	20
α-helix	81-83	3
β-strand	86-91	6	21
β-strand	100-101	2	21
β-strand	105-109	5	21
β-strand	114	1	22
α-helix	115-116	2
β-strand	117-121	5	23
α-helix	122-124	3
α-helix	125-130	6
β-strand	132-142	11	23
β-strand	143	1	22
β-strand	148-153	6	24
β-strand	156-157	2	24
β-strand	162-166	5	23
α-helix	167-170	4
β-strand	176-185	10	23
α-helix	186-189	4
β-strand	194-200	7	24
β-strand	208-213	6	24

Chain g: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	35-44	10

6 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, G, H	protein	354	Saccharomyces cerevisiae (ATCC 204508 / S288c)	Q12154 (AlphaFold model)
Antibody heavy chain	C, E, I, K	protein	230	Homo sapiens, synthetic construct
Antibody light chain	D, F, J, L	protein	217	Homo sapiens, synthetic construct
Nyv1 TMD	a, g	protein	37	Saccharomyces cerevisiae

Sequence of entity 1 (A, B, G, H), FASTA

>4XVU_1 ATPase GET3 (chains A, B, G, H)
MDLTVEPNLHSLITSTTHKWIFVGGKGGVGKTTSSCSIAIQMALSQPNKQFLLISTNPAH
NLSDAFGEKFGKDARKVTGMNNLSCMEIDPSAALKDMNDMAVSRANNNGSDGQGDDLGSL
LQGGALADLTGSIPGIDEALSFMEVMKHIKRQEQGEGETFDTVIFDTAPTGHTLRFLQLP
NTLSKLLEKFGEITNKLGPMLNSFMGAGNVDISGKLNELKANVETIRQQFTDPDLTTFVC
VCISEFLSLYETERLIQELISYDMDVNSIIVNQLLFAENDQEHNCKRCQARWKMQKKYLD
QIDELYEDFHVVKMPLCAGEIRGLNNLTKFSQFLNKEYNPITDGKVIYELEDKE

Sequence of entity 2 (C, E, I, K), FASTA

>4XVU_2 Antibody heavy chain (chains C, E, I, K)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNLYYYSIHWVRQAPGKGLEWVASISPYSSS
TSYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARGRWYRRALDYWGQGTLVTV
SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT

Sequence of entity 3 (D, F, J, L), FASTA

>4XVU_3 Antibody light chain (chains D, F, J, L)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQYPYYSSLITFGQGTKVEIKRTVAAPSVFI
FPPSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSS
TLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 4 (a, g), FASTA

>4XVU_4 Nyv1 TMD (chains a, g)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	4
MG	Magnesium ion	Mg	4
ZN	Zinc ion	Zn	2

Primary citation

Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo. Mateja, A., Paduch, M., Chang, H.Y. et al. Science (2015) 347:1152-1155. DOI 10.1126/science.1261671 · 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
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
9NS5 3.19 Å, Get3(D57N)-Get4/5 Complex (ATP-bound)

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