2PM7: Protein transport protein SEC31

Name: PDB 2PM7: Crystal structure of yeast Sec13/31 edge element of the COPII vesicular coat, selenomethionine version
Published: 2007-07-03
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: protein transport

Crystal structure of yeast Sec13/31 edge element of the COPII vesicular coat, selenomethionine version. Determined by X-ray diffraction at 2.35 Å resolution. Released 3 Jul 2007.

Method: X-ray diffraction
Resolution: 2.35 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 10,195
Mol. weight: 157.29 kDa
Released: 3 Jul 2007

Explore 2PM7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2PM7 contains 52 α-helices and 70 β-strands across 4 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: 20 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	385-387	3	1
β-strand	391-395	5	1
β-strand	402-405	4	1
α-helix	416-424	9
α-helix	428-436	9
α-helix	441-456	16
α-helix	458-466	9
β-strand	504	1	2
α-helix	509-519	11
α-helix	523-531	9
α-helix	536-543	8
α-helix	549-563	15
α-helix	568-577	10
α-helix	582-587	6
β-strand	588	1	3
α-helix	590-592	3
α-helix	593-603	11
α-helix	608-623	16
α-helix	628-638	11
α-helix	641-650	10
α-helix	652-661	10
α-helix	666-685	20
α-helix	697-711	15
α-helix	716-725	10
α-helix	731-744	14

Chain B: 5 helices, 31 β-strands

Element	Residues	Length	Sheet
β-strand	3-4	2	1
β-strand	12-17	6	4
β-strand	23-28	6	4
β-strand	33-37	5	4
β-strand	38	1	5
β-strand	43	1	5
β-strand	47-49	3	4
β-strand	56-61	6	6
α-helix	62-63	2
α-helix	64-66	3
β-strand	69-74	6	6
β-strand	78-83	6	6
β-strand	84	1	7
β-strand	89	1	7
β-strand	93-95	3	6
β-strand	102-107	6	8
α-helix	110-112	3
β-strand	115-120	6	8
β-strand	124-129	6	8
β-strand	130	1	9
β-strand	136	1	9
β-strand	139-142	4	8
β-strand	148-153	6	10
α-helix	154-156	3
β-strand	172-177	6	10
β-strand	182-188	7	10
β-strand	193-200	8	10
β-strand	207-212	6	11
β-strand	220-226	7	11
β-strand	231-236	6	11
β-strand	244-247	4	11
α-helix	252-253	2
β-strand	257-262	6	12
β-strand	269-273	5	12
β-strand	278-283	6	12
β-strand	289-291	3	12

Chain C: 20 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	385-387	3	13
β-strand	391-395	5	13
β-strand	402-405	4	13
β-strand	409	1	14
β-strand	412	1	14
α-helix	416-424	9
α-helix	428-436	9
α-helix	441-456	16
α-helix	458-466	9
β-strand	504	1	3
α-helix	509-519	11
α-helix	523-532	10
α-helix	536-543	8
α-helix	550-563	14
α-helix	568-577	10
α-helix	582-587	6
β-strand	588	1	2
α-helix	590-592	3
α-helix	593-603	11
α-helix	608-624	17
α-helix	628-637	10
α-helix	641-650	10
α-helix	652-661	10
α-helix	666-687	22
α-helix	697-711	15
α-helix	716-723	8
α-helix	731-744	14

Chain D: 7 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	3-4	2	13
α-helix	11	1
β-strand	12-17	6	15
β-strand	23-28	6	15
β-strand	33-38	6	15
β-strand	43-49	7	15
β-strand	56-61	6	16
α-helix	62-63	2
β-strand	65	1	17
β-strand	67	1	17
β-strand	69-74	6	16
β-strand	79-84	6	16
β-strand	89-95	7	16
β-strand	102-107	6	18
α-helix	108-109	2
α-helix	110-112	3
β-strand	116-120	5	18
β-strand	124-130	7	18
β-strand	136-142	7	18
β-strand	148-153	6	19
α-helix	154-157	4
α-helix	168-170	3
β-strand	172-177	6	19
β-strand	182-188	7	19
β-strand	193-200	8	19
β-strand	207-212	6	20
β-strand	220-226	7	20
β-strand	231-236	6	20
α-helix	242-243	2
β-strand	244-247	4	20
β-strand	257-262	6	21
β-strand	269-273	5	21
β-strand	278-283	6	21
β-strand	289-291	3	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein transport protein SEC31	A, C	protein	399	Saccharomyces cerevisiae	P38968 (AlphaFold model)
Protein transport protein SEC13	B, D	protein	297	Saccharomyces cerevisiae	Q04491 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>2PM7_1 Protein transport protein SEC31 (chains A, C)
GAMGSHLQAPTWYGEPSPAAHWAFGGKLVQITPDGKGVSITNPKISGLESNTTLSEALKT
KDFKPLINQRLVKVIDDVNEEDWNMLEKLSMDGTEEFLKEALAFDNDESDAQDDANNEKE
DDGEEFFQQIETNFQPEGDFSLSGNIEQTISKNLVSGNIKSAVKNSLENDLMMEAMVIAL
DSNNERLKESVKNAYFAKYGSKSSLSRILYSISKREVDDLVENLDVSQWKFISKAIQNLY
PNDIAQRNEMMIKLGDRMKENGHRQDSLTLYLAAGSLDKVASIWLSEFPDLEDKLKKDNK
TIYEAHSECMTEFIERFTVFSNFINGSSTINNEQLIAKFLEFINLTTSTGNFELATEFLN
SLPSDNEEVKTEKARVLIASGKSLPAQNPATATTSKAKY

Sequence of entity 2 (B, D), FASTA

>2PM7_2 Protein transport protein SEC13 (chains B, D)
MVVIANAHNEMIHDAVMDYYGKRMATCSSDKTIKIFEVEGETHKLIDTLTGHEGPVWRVD
WAHPKFGTILASCSYDGKVMIWKEENGRWSQIAVHAVHSASVNSVQWAPHEYGPMLLVAS
SDGKVSVVEFKENGTTSPIIIDAHAIGVNSASWAPATIEEDGEHNGTKESRKFVTGGADN
LVKIWKYNSDAQTYVLESTLEGHSDWVRDVAWSPTVLLRSYMASVSQDRTCIIWTQDNEQ
GPWKKTLLKEEKFPDVLWRASWSLSGNVLALSGGDNKVTLWKENLEGKWEPAGEVHQ

Primary citation

Structure and Organization of Coat Proteins in the COPII Cage. Fath, S., Mancias, J.D., Bi, X. et al. Cell (2007) 129:1325-1336. DOI 10.1016/j.cell.2007.05.036 · PubMed

Other PDB entries of the same protein (UniProt P38968 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2PM6 2.45 Å, Crystal Structure of yeast Sec13/31 edge element of the COPII vesicular coat, native…
2QTV 2.5 Å, Structure of Sec23-Sar1 complexed with the active fragment of Sec31
3MZL 2.8 Å, Sec13/Sec31 edge element, loop deletion mutant
2PM9 3.3 Å, Crystal structure of yeast Sec13/31 vertex element of the COPII vesicular coat
6ZG6 12.0 Å, COPII on membranes, outer coat vertex
4BZJ 40.0 Å, The structure of the COPII coat assembled on membranes
4BZK 40.0 Å, The structure of the COPII coat assembled on membranes
6ZG5 40.0 Å, COPII on membranes, outer coat right-handed rod, class1
6ZL0 40.0 Å, COPII on membranes, outer coat left-handed rod

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