4F91: Brr2 Helicase Region

Brr2 Helicase Region. Determined by X-ray diffraction at 2.7 Å resolution. Released 17 Oct 2012.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 1
Atoms: 13,865
Mol. weight: 197.24 kDa
Released: 17 Oct 2012

Explore 4F91 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4F91 contains 92 α-helices and 68 β-strands across 1 chain. 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 B: 92 helices, 68 β-strands

Element	Residues	Length	Sheet
α-helix	411-414	4
α-helix	419-421	3
β-strand	436-438	3	1
β-strand	442-447	6	1
α-helix	448-452	5
β-strand	463	1	2
α-helix	464-466	3
α-helix	469-472	4
β-strand	480	1	2
α-helix	483-494	12
β-strand	499-503	5	3
α-helix	510-521	12
β-strand	537-541	5	3
α-helix	545-558	14
β-strand	566-568	3	3
β-strand	585-588	4	3
α-helix	590-596	7
α-helix	601-604	4
β-strand	609-614	6	3
α-helix	617-620	4
α-helix	625-642	18
β-strand	647-653	7	3
α-helix	658-664	7
α-helix	669-672	4
β-strand	673-675	3	3
α-helix	678-680	3
β-strand	685-692	8	1
α-helix	697-712	16
β-strand	721-725	5	1
α-helix	730-733	4
α-helix	736-739	4
α-helix	761-765	5
α-helix	772-777	6
β-strand	782-785	4	1
α-helix	794-802	9
β-strand	808-812	5	1
α-helix	813-818	6
β-strand	823	1	4
β-strand	825-829	5	1
β-strand	833-835	3	5
β-strand	840-842	3	5
α-helix	843-845	3
α-helix	846-852	7
α-helix	853-855	3
β-strand	856	1	4
β-strand	865-870	6	1
α-helix	878-883	6
α-helix	897-907	11
β-strand	912	1	6
α-helix	913-920	8
α-helix	924-931	8
α-helix	940-945	6
α-helix	950-966	17
β-strand	970-972	3	7
β-strand	978	1	6
β-strand	979-981	3	7
α-helix	983-991	9
α-helix	995-1004	10
α-helix	1011-1019	9
α-helix	1022-1024	3
α-helix	1031-1033	3
α-helix	1034-1043	10
α-helix	1055-1067	13
α-helix	1075-1100	26
β-strand	1104	1	8
α-helix	1105-1120	16
α-helix	1128-1131	4
α-helix	1137-1145	9
α-helix	1150-1153	4
α-helix	1158-1165	8
α-helix	1168-1170	3
α-helix	1171-1178	8
β-strand	1184-1192	9	9
β-strand	1197-1206	10	9
β-strand	1218-1226	9	10
β-strand	1232	1	8
β-strand	1233-1242	10	10
β-strand	1250-1257	8	9
β-strand	1265-1272	8	10
β-strand	1279-1285	7	10
α-helix	1291-1300	10
α-helix	1304-1307	4
β-strand	1308	1	11
α-helix	1309-1311	3
α-helix	1315-1322	8
β-strand	1327	1	11
α-helix	1330-1340	11
β-strand	1346-1349	4	12
α-helix	1356-1370	15
β-strand	1376-1379	4	12
α-helix	1383-1393	11
α-helix	1394-1399	6
β-strand	1405-1407	3	12
α-helix	1412-1421	10
β-strand	1424-1427	4	12
α-helix	1429-1436	8
β-strand	1450-1454	5	12
α-helix	1456-1460	5
α-helix	1464-1480	17
α-helix	1484-1485	2
β-strand	1486-1491	6	12
β-strand	1494	1	13
α-helix	1497-1504	8
β-strand	1511-1513	3	12
α-helix	1516-1518	3
β-strand	1523-1530	8	14
α-helix	1535-1540	6
α-helix	1543-1553	11
β-strand	1559-1563	5	14
α-helix	1566-1582	17
β-strand	1590	1	15
α-helix	1594-1601	8
α-helix	1607-1614	8
β-strand	1617-1620	4	14
α-helix	1626-1638	13
β-strand	1641	1	15
β-strand	1643-1647	5	14
α-helix	1648-1650	3
β-strand	1658	1	16
β-strand	1660-1664	5	14
β-strand	1667-1670	4	17
β-strand	1675-1678	4	17
α-helix	1679-1680	2
α-helix	1681-1688	8
β-strand	1691	1	16
β-strand	1700-1707	8	14
α-helix	1708-1719	12
α-helix	1721	1
β-strand	1722	1	13
α-helix	1723-1724	2
α-helix	1728-1730	3
α-helix	1732-1741	10
β-strand	1747	1	18
α-helix	1748-1754	7
α-helix	1755-1757	3
α-helix	1759-1766	8
α-helix	1768-1771	4
α-helix	1778-1798	21
β-strand	1802-1805	4	18
β-strand	1809-1812	4	18
α-helix	1814-1822	9
α-helix	1826-1835	10
α-helix	1842-1850	9
α-helix	1853-1855	3
α-helix	1864-1872	9
α-helix	1887-1899	13
α-helix	1906-1931	26
α-helix	1936-1950	15
α-helix	1959-1962	4
α-helix	1968-1975	8
α-helix	1990-1993	4
α-helix	2001-2010	10
β-strand	2017-2018	2	19
β-strand	2021-2023	3	19
β-strand	2034-2043	10	19
β-strand	2064-2070	7	20
β-strand	2075-2082	8	20
β-strand	2087-2095	9	19
β-strand	2102-2110	9	20
β-strand	2118-2124	7	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
U5 small nuclear ribonucleoprotein 200 kDa helicase	B	protein	1724	Homo sapiens	O75643 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>4F91_1 U5 small nuclear ribonucleoprotein 200 kDa helicase (chains B)
ALAPRQVLDLEDLVFTQGSHFMANKRCQLPDGSFRRQRKGYEEVHVPALKPKPFGSEEQL
LPVEKLPKYAQAGFEGFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREI
GKHINMDGTINVDDFKIIYIAPMRSLVQEMVGSFGKRLATYGITVAELTGDHQLCKEEIS
ATQIIVCTPEKWDIITRKGGERTYTQLVRLIILDEIHLLHDDRGPVLEALVARAIRNIEM
TQEDVRLIGLSATLPNYEDVATFLRVDPAKGLFYFDNSFRPVPLEQTYVGITEKKAIKRF
QIMNEIVYEKIMEHAGKNQVLVFVHSRKETGKTARAIRDMCLEKDTLGLFLREGSASTEV
LRTEAEQCKNLELKDLLPYGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNL
PAHTVIIKGTQVYSPEKGRWTELGALDILQMLGRAGRPQYDTKGEGILITSHGELQYYLS
LLNQQLPIESQMVSKLPDMLNAEIVLGNVQNAKDAVNWLGYAYLYIRMLRSPTLYGISHD
DLKGDPLLDQRRLDLVHTAALMLDKNNLVKYDKKTGNFQVTELGRIASHYYITNDTVQTY
NQLLKPTLSEIELFRVFSLSSEFKNITVREEEKLELQKLLERVPIPVKESIEEPSAKINV
LLQAFISQLKLEGFALMADMVYVTQSAGRLMRAIFEIVLNRGWAQLTDKTLNLCKMIDKR
MWQSMCPLRQFRKLPEEVVKKIEKKNFPFERLYDLNHNEIGELIRMPKMGKTIHKYVHLF
PKLELSVHLQPITRSTLKVELTITPDFQWDEKVHGSSEAFWILVEDVDSEVILHHEYFLL
KAKYAQDEHLITFFVPVFEPLPPQYFIRVVSDRWLSCETQLPVSFRHLILPEKYPPPTEL
LDLQPLPVSALRNSAFESLYQDKFPFFNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAE
FAILRMLLQSSEGRCVYITPMEALAEQVYMDWYEKFQDRLNKKVVLLTGETSTDLKLLGK
GNIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVHLIGGENGPVLEVICSRMRYISSQI
ERPIRIVALSSSLSNAKDVAHWLGCSATSTFNFHPNVRPVPLELHIQGFNISHTQTRLLS
MAKPVYHAITKHSPKKPVIVFVPSRKQTRLTAIDILTTCAADIQRQRFLHCTEKDLIPYL
EKLSDSTLKETLLNGVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVAAHLV
IIMDTQYYNGKIHAYVDYPIYDVLQMVGHANRPLQDDEGRCVIMCQGSKKDFFKKFLYEP
LPVESHLDHCMHDHFNAEIVTKTIENKQDAVDYLTWTFLYRRMTQNPNYYNLQGISHRHL
SDHLSELVEQTLSDLEQSKCISIEDEMDVAPLNLGMIAAYYYINYTTIELFSMSLNAKTK
VRGLIEIISNAAEYENIPIRHHEDNLLRQLAQKVPHKLNNPKFNDPHVKTNLLLQAHLSR
MQLSAELQSDTEEILSKAIRLIQACVDVLSSNGWLSPALAAMELAQMVTQAMWSKDSYLK
QLPHFTSEHIKRCTDKGVESVFDIMEMEDEERNALLQLTDSQIADVARFCNRYPNIELSY
EVVDKDSIRSGGPVVVLVQLEREEEVTGPVIAPLFPQKREEGWWVVIGDAKSNSLISIKR
LTLQQKAKVKLDFVAPATGAHNYTLYFMSDAYMGCDQEYKFSVD

Primary citation

Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome. Santos, K.F., Jovin, S.M., Weber, G. et al. Proc Natl Acad Sci U S A (2012) 109:17418-17423. DOI 10.1073/pnas.1208098109 · PubMed

Other PDB entries of the same protein (UniProt O75643 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2Q0Z 2.0 Å, Crystal structure of Q9P172/Sec63 from Homo sapiens. Northeast Structural Genomics…
8BCE 2.05 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 76
8BC9 2.3 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 24
8BCC 2.35 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 39
8BCB 2.38 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 34
8BC8 2.39 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 18
8BCG 2.39 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 86
6S8Q 2.39 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1
9S2E 2.4 Å, Human intron-lariat spliceosome-Aquarius (ILSaqr)
8BCF 2.42 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 78
7BDK 2.52 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and ADP
7BDJ 2.59 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and mant-ATPgammaS

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