2QTV: Sec23-Sar1

Structure of Sec23-Sar1 complexed with the active fragment of Sec31. Determined by X-ray diffraction at 2.5 Å resolution. Released 15 Jan 2008.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Saccharomyces cerevisiae
Chains: 3
Atoms: 7,619
Mol. weight: 110.4 kDa
Ligands: ZN, MG, GNP
Released: 15 Jan 2008

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

Secondary structure: helices and β-sheets

2QTV contains 44 α-helices and 50 β-strands across 3 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: 33 helices, 42 β-strands

Element	Residues	Length	Sheet
α-helix	3-10	8
β-strand	12-14	3	1
β-strand	16	1	2
β-strand	18-20	3	3
α-helix	23-28	6
α-helix	32	1
β-strand	33-37	5	1
β-strand	48-49	2	3
β-strand	55	1	4
β-strand	64	1	4
α-helix	69-70	2
β-strand	71-72	2	5
β-strand	77-79	3	5
β-strand	86-88	3	5
α-helix	89-90	2
α-helix	103-106	4
β-strand	109-117	9	3
α-helix	118	1
β-strand	123-129	7	6
α-helix	134-148	15
β-strand	156-162	7	6
β-strand	165-170	6	6
β-strand	178-183	6	6
α-helix	190-198	9
α-helix	224-227	4
β-strand	229-230	2	6
α-helix	231-244	14
β-strand	256	1	7
α-helix	262-276	15
β-strand	282-288	7	6
β-strand	303	1	7
α-helix	307-309	3
α-helix	311-315	5
α-helix	322-339	18
β-strand	341-348	8	6
α-helix	355-358	4
α-helix	360-363	4
β-strand	369-372	4	6
α-helix	378-386	9
β-strand	390	1	8
β-strand	396	1	8
β-strand	399-408	10	3
β-strand	412-418	7	1
β-strand	422-423	2	3
β-strand	432	1	1
β-strand	439	1	1
β-strand	444-450	7	3
β-strand	456-462	7	1
β-strand	484-495	12	3
β-strand	499-512	14	3
α-helix	517-521	5
β-strand	523	1	2
α-helix	525-540	16
α-helix	545-563	19
β-strand	565-567	3	9
β-strand	570-575	6	9
α-helix	583-591	9
α-helix	603-613	11
α-helix	618-625	8
β-strand	628-632	5	10
β-strand	639-640	2	10
β-strand	644	1	11
α-helix	645-647	3
β-strand	653-657	5	10
β-strand	661-666	6	10
α-helix	668-676	9
α-helix	678-680	3
α-helix	686-702	17
α-helix	708-709	2
β-strand	710-715	6	10
α-helix	719-721	3
α-helix	722-725	4
β-strand	729	1	11
α-helix	749-751	3
α-helix	752-763	12

Chain B: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	25-29	5	12
α-helix	36-45	10
α-helix	52-54	3
β-strand	58-62	5	12
β-strand	69-73	5	12
α-helix	78-87	10
β-strand	93-99	7	12
α-helix	103-105	3
α-helix	106-117	12
β-strand	127-132	6	12
α-helix	142-149	8
α-helix	164-165	2
β-strand	166-171	6	12
β-strand	172	1	13
β-strand	177	1	13
α-helix	179-186	8

Chain D: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	916-919	4
α-helix	921	1
α-helix	934-939	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein transport protein SEC23	A	protein	772	Saccharomyces cerevisiae	P15303 (AlphaFold model)
Small COPII coat GTPase SAR1	B	protein	167	Saccharomyces cerevisiae	P20606 (AlphaFold model)
Protein transport protein SEC31	D	protein	49	Saccharomyces cerevisiae	P38968 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2QTV_1 Protein transport protein SEC23 (chains A)
GAMGSDFETNEDINGVRFTWNVFPSTRSDANSNVVPVGCLYTPLKEYDELNVAPYNPVVC
SGPHCKSILNPYCVIDPRNSSWSCPICNSRNHLPPQYTNLSQENMPLELQSTTIEYITNK
PVTVPPIFFFVVDLTSETENLDSLKESIITSLSLLPPNALIGLITYGNVVQLHDLSSETI
DRCNVFRGDREYQLEALTEMLTGQKPTGPGGAASHLPNAMNKVTPFSLNRFFLPLEQVEF
KLNQLLENLSPDQWSVPAGHRPLRATGSALNIASLLLQGCYKNIPARIILFASGPGTVAP
GLIVNSELKDPLRSHHDIDSDHAQHYKKACKFYNQIAQRVAANGHTVDIFAGCYDQIGMS
EMKQLTDSTGGVLLLTDAFSTAIFKQSYLRLFAKDEEGYLKMAFNGNMAVKTSKDLKVQG
LIGHASAVKKTDANNISESEIGIGATSTWKMASLSPYHSYAIFFEIANTAANSNPMMSAP
GSADRPHLAYTQFITTYQHSSGTNRIRVTTVANQLLPFGTPAIAASFDQEAAAVLMARIA
VHKAETDDGADVIRWLDRTLIKLCQKYADYNKDDPQSFRLAPNFSLYPQFTYYLRRSQFL
SVFNNSPDETAFYRHIFTREDTTNSLIMIQPTLTSFSMEDDPQPVLLDSISVKPNTILLL
DTFFFILIYHGEQIAQWRKAGYQDDPQYADFKALLEEPKLEAAELLVDRFPLPRFIDTEA
GGSQARFLLSKLNPSDNYQDMARGGSTIVLTDDVSLQNFMTHLQQVAVSGQA

Sequence of entity 2 (B), FASTA

>2QTV_2 Small COPII coat GTPase SAR1 (chains B)
HGKLLFLGLDNAGKTTLLHMLKNDRLATLQPTWHPTSEELAIGNIKFTTFDLGGHIQARR
LWKDYFPEVNGIVFLVDAADPERFDEARVELDALFNIAELKDVPFVILGNKIDAPNAVSE
AELRSALGLLNTTGSQRIEGQRPVEVFMCSVVMRNGYLEAFQWLSQY

Sequence of entity 3 (D), FASTA

>2QTV_3 Protein transport protein SEC31 (chains D)
PSQPPINAVSGQTPHLNRKANDGWNDLPLKVKEKPSRAKAVSVAPPNIL

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1
MG	Magnesium ion	Mg	1
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	1

Primary citation

Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31. Bi, X., Mancias, J.D., Goldberg, J. Dev Cell (2007) 13:635-645. DOI 10.1016/j.devcel.2007.10.006 · PubMed

Other PDB entries of the same protein (UniProt P15303 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1M2O 2.5 Å, Crystal Structure of the Sec23-Sar1 complex
1M2V 2.75 Å, Crystal Structure of the yeast Sec23/24 heterodimer
8BSH 3.8 Å, COPII inner coat
6ZGA 4.6 Å, COPII on membranes, inner coat
6GNI 4.9 Å, Cryo-tomography and subtomogram averaging of Sar1-Sec23-Sec24 - fitted model.
4BZI 23.0 Å, The structure of the COPII coat assembled on membranes

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