6F7P: Human ARS2 residues 147-270 + 408-763

Crystal structure of Human ARS2 residues 147-270 + 408-763. Determined by X-ray diffraction at 3.7 Å resolution. Released 9 May 2018.

Method: X-ray diffraction
Resolution: 3.7 Å
Organism: Homo sapiens
Chains: 4
Atoms: 7,259
Mol. weight: 111.85 kDa
Released: 9 May 2018

Explore 6F7P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6F7P contains 56 α-helices and 38 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: 7 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	152-157	6
α-helix	165-190	26
α-helix	195-201	7
α-helix	203-230	28
β-strand	239	1	1
α-helix	243-258	16
α-helix	262-265	4
α-helix	266-268	3

Chain B: 8 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	149-151	3
α-helix	152-157	6
α-helix	165-190	26
α-helix	195-201	7
α-helix	203-230	28
β-strand	239	1	9
α-helix	243-258	16
α-helix	262-265	4
α-helix	266-268	3

Chain C: 20 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	421-427	7	2
α-helix	433-441	9
β-strand	446-451	6	2
α-helix	453-454	2
β-strand	455	1	3
α-helix	456-458	3
β-strand	461	1	3
β-strand	462-468	7	2
α-helix	475-480	6
β-strand	485-486	2	4
β-strand	489-490	2	4
β-strand	494-496	3	2
α-helix	497-499	3
β-strand	503-505	3	5
α-helix	508-510	3
α-helix	513-534	22
α-helix	555-562	8
α-helix	570-575	6
α-helix	602-617	16
β-strand	621-622	2	6
β-strand	627-628	2	6
β-strand	642-644	3	5
β-strand	645	1	1
α-helix	652-654	3
α-helix	657-669	13
α-helix	670-673	4
α-helix	674-676	3
β-strand	678	1	7
α-helix	679-680	2
α-helix	681-687	7
α-helix	689-691	3
α-helix	692-703	12
β-strand	705-708	4	8
β-strand	711-714	4	8
β-strand	719-721	3	8
α-helix	724-734	11
α-helix	736-754	19
β-strand	755	1	7

Chain D: 21 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	421-427	7	10
α-helix	433-441	9
β-strand	446-451	6	10
α-helix	453-454	2
β-strand	455	1	11
α-helix	456-458	3
β-strand	461	1	11
β-strand	462-468	7	10
α-helix	475-480	6
β-strand	485-486	2	12
β-strand	489-490	2	12
β-strand	494-496	3	10
α-helix	497-499	3
β-strand	503-505	3	13
α-helix	508-510	3
α-helix	513-534	22
α-helix	555-557	3
α-helix	561-564	4
α-helix	570-576	7
α-helix	602-617	16
β-strand	621-622	2	14
β-strand	627-628	2	14
β-strand	642-644	3	13
β-strand	645	1	9
α-helix	652-654	3
α-helix	657-669	13
α-helix	670-673	4
α-helix	674-676	3
β-strand	678	1	15
α-helix	679-680	2
α-helix	681-687	7
α-helix	689-691	3
α-helix	692-703	12
β-strand	705-708	4	16
β-strand	711-714	4	16
β-strand	719-721	3	16
α-helix	724-734	11
α-helix	736-754	19
β-strand	755	1	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serrate RNA effector molecule homolog	A, B	protein	124	Homo sapiens	Q9BXP5 (AlphaFold model)
Serrate RNA effector molecule homolog	C, D	protein	356	Homo sapiens	Q9BXP5 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6F7P_1 Serrate RNA effector molecule homolog (chains A, B)
PVMKTFKEFLLSLDDSVDETEAVKRYNDYKLDFRRQQMQDFFLAHKDEEWFRSKYHPDEV
GKRRQEARGALQNRLRVFLSLMETGWFDNLLLDIDKADAIVKMLDAAVIKMEGGTENDLR
ILEQ

Sequence of entity 2 (C, D), FASTA

>6F7P_2 Serrate RNA effector molecule homolog (chains C, D)
GLECKPRPLHKTCSLFMRNIAPNISRAEIISLCKRYPGFMRVALSEPQPERRFFRRGWVT
FDRSVNIKEICWNLQNIRLRECELSPGVNRDLTRRVRNINGITQHKQIVRNDIKLAAKLI
HTLDDRTQLWASEPGTPPLPTSLPSQNPILKNITDYLIEEVSAEEEELLGSSGGAPPEEP
PKEGNPAEINVERDEKLIKVLDKLLLYLRIVHSLDYYNTCEYPNEDEMPNRCGIIHVRGP
MPPNRISHGEVLEWQKTFEEKLTPLLSVRESLSEEEAQKMGRKDPEQEVEKFVTSNTQEL
GKDKWLCPLSGKKFKGPEFVRKHIFNKHAEKIEEVKKEVAFFNNFLTDAKRPALPE

Primary citation

Structural analysis of human ARS2 as a platform for co-transcriptional RNA sorting. Schulze, W.M., Stein, F., Rettel, M. et al. Nat Commun (2018) 9:1701-1701. DOI 10.1038/s41467-018-04142-7 · PubMed

Other PDB entries of the same protein (UniProt Q9BXP5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5OO6 2.8 Å, Complex of human nuclear cap-binding complex with ARS2 C-terminal peptide
6F7J 3.22 Å, Crystal structure of Human ARS2 residues 171-270 + 408-763
6F7S 3.37 Å, Crystal structure of Human ARS2 residues 147-270 + 408-763 with deletion of loop B
8PMP 3.43 Å, Structure of the human nuclear cap-binding complex bound to ARS2[147-871] and m7GTP
6F8D 3.48 Å, Crystal structure of Human ARS2 residues 171-270 + 408-763 (P65 form)

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