4F92: Brr2 Helicase Region S1087L

Brr2 Helicase Region S1087L. Determined by X-ray diffraction at 2.66 Å resolution. Released 17 Oct 2012.

Method
X-ray diffraction
Resolution
2.66 Å
Organism
Homo sapiens
Chains
1
Atoms
14,019
Mol. weight
197.44 kDa
Ligands
SAN
Released
17 Oct 2012

Explore 4F92 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4F92 contains 95 α-helices and 71 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: 95 helices, 71 β-strands

ElementResiduesLengthSheet
α-helix411-4144
α-helix419-4213
β-strand436-43831
β-strand442-44541
β-strand446-44722
α-helix448-4558
β-strand46313
α-helix469-4713
β-strand48013
α-helix483-4875
α-helix489-4935
β-strand499-50244
α-helix510-52112
α-helix522-5243
β-strand537-54154
α-helix545-55915
β-strand566-56834
α-helix580-5823
β-strand585-58844
α-helix590-5967
α-helix603-6064
β-strand609-61464
α-helix617-6215
α-helix625-64218
β-strand647-65264
α-helix658-6647
α-helix669-6724
β-strand673-67534
α-helix678-6803
β-strand685-68842
β-strand691-69221
α-helix697-71216
β-strand721-72442
α-helix732-74413
α-helix761-7644
α-helix772-7776
β-strand782-78542
α-helix792-80211
β-strand808-81142
α-helix813-8186
β-strand82315
β-strand825-82952
β-strand832-83546
β-strand840-84346
α-helix844-8452
α-helix846-8538
β-strand85615
β-strand865-87062
β-strand871-87221
α-helix878-8825
α-helix897-90711
β-strand91217
α-helix913-92210
α-helix924-9318
α-helix940-9456
α-helix950-96617
β-strand970-97238
β-strand97817
β-strand979-98138
α-helix983-9908
α-helix995-100410
α-helix1011-10199
α-helix1022-10243
α-helix1031-10333
α-helix1034-104310
α-helix1055-106713
α-helix1075-110127
β-strand110419
α-helix1105-112016
α-helix1128-11314
α-helix1137-11448
α-helix1150-11556
α-helix1158-11658
α-helix1171-11788
β-strand1184-1192910
β-strand1197-12061010
β-strand1218-1226911
β-strand123219
β-strand1233-12421011
α-helix1243-12453
β-strand1250-1257810
β-strand1265-1272811
β-strand1279-1285711
α-helix1291-130111
α-helix1304-13074
β-strand1308112
α-helix1309-13113
α-helix1315-13184
β-strand1327112
α-helix1330-134011
β-strand1346-1349413
α-helix1357-137014
β-strand1376-1379413
α-helix1383-139311
α-helix1394-14007
β-strand1405-1407313
α-helix1412-142110
β-strand1424-1427413
α-helix1429-14368
α-helix1443-14464
β-strand1450-1453413
α-helix1456-14605
α-helix1464-147916
α-helix14851
β-strand1486-1491613
β-strand1494114
α-helix1497-15048
β-strand1511-1513313
α-helix1516-15183
β-strand1523-1530815
α-helix1535-15406
α-helix1543-155311
β-strand1559-1563515
α-helix1566-158217
β-strand1590116
α-helix1594-16018
α-helix1607-16148
β-strand1617-1620415
α-helix1626-163813
β-strand1641116
β-strand1643-1647515
α-helix1648-16503
β-strand1658117
β-strand1660-1664515
β-strand1667-1670418
β-strand1675-1678418
α-helix1679-16802
α-helix1681-16888
β-strand1691117
β-strand1700-1707815
α-helix1708-17103
α-helix1711-17177
α-helix17211
β-strand1722114
α-helix17231
α-helix1728-17303
α-helix1733-17419
β-strand1747119
α-helix1748-17558
α-helix1760-17667
α-helix1768-17703
α-helix1778-179821
β-strand1802-1805419
β-strand1809-1812419
α-helix1814-18218
α-helix1826-183510
α-helix1842-18509
α-helix1853-18553
α-helix1864-187411
α-helix1887-189913
α-helix1906-193227
β-strand1935120
α-helix1936-195015
α-helix1959-19624
α-helix1968-197710
α-helix1982-19865
α-helix1990-19934
α-helix2001-201313
β-strand2017-2024821
β-strand2034-20431021
α-helix2050-20523
β-strand2064-2070720
β-strand2075-2082820
β-strand2087-2095921
β-strand2102-2110920
β-strand2118-2124720

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
U5 small nuclear ribonucleoprotein 200 kDa helicaseBprotein1724Homo sapiensO75643 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>4F92_1 U5 small nuclear ribonucleoprotein 200 kDa helicase (chains B)
ALAPRQVLDLEDLVFTQGSHFMANKRCQLPDGSFRRQRKGYEEVHVPALKPKPFGSEEQL
LPVEKLPKYAQAGFEGFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREI
GKHINMDGTINVDDFKIIYIAPMRSLVQEMVGSFGKRLATYGITVAELTGDHQLCKEEIS
ATQIIVCTPEKWDIITRKGGERTYTQLVRLIILDEIHLLHDDRGPVLEALVARAIRNIEM
TQEDVRLIGLSATLPNYEDVATFLRVDPAKGLFYFDNSFRPVPLEQTYVGITEKKAIKRF
QIMNEIVYEKIMEHAGKNQVLVFVHSRKETGKTARAIRDMCLEKDTLGLFLREGSASTEV
LRTEAEQCKNLELKDLLPYGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNL
PAHTVIIKGTQVYSPEKGRWTELGALDILQMLGRAGRPQYDTKGEGILITSHGELQYYLS
LLNQQLPIESQMVSKLPDMLNAEIVLGNVQNAKDAVNWLGYAYLYIRMLRSPTLYGISHD
DLKGDPLLDQRRLDLVHTAALMLDKNNLVKYDKKTGNFQVTELGRIASHYYITNDTVQTY
NQLLKPTLSEIELFRVFSLSSEFKNITVREEEKLELQKLLERVPIPVKESIEEPSAKINV
LLQAFISQLKLEGFALMADMVYVTQLAGRLMRAIFEIVLNRGWAQLTDKTLNLCKMIDKR
MWQSMCPLRQFRKLPEEVVKKIEKKNFPFERLYDLNHNEIGELIRMPKMGKTIHKYVHLF
PKLELSVHLQPITRSTLKVELTITPDFQWDEKVHGSSEAFWILVEDVDSEVILHHEYFLL
KAKYAQDEHLITFFVPVFEPLPPQYFIRVVSDRWLSCETQLPVSFRHLILPEKYPPPTEL
LDLQPLPVSALRNSAFESLYQDKFPFFNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAE
FAILRMLLQSSEGRCVYITPMEALAEQVYMDWYEKFQDRLNKKVVLLTGETSTDLKLLGK
GNIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVHLIGGENGPVLEVICSRMRYISSQI
ERPIRIVALSSSLSNAKDVAHWLGCSATSTFNFHPNVRPVPLELHIQGFNISHTQTRLLS
MAKPVYHAITKHSPKKPVIVFVPSRKQTRLTAIDILTTCAADIQRQRFLHCTEKDLIPYL
EKLSDSTLKETLLNGVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVAAHLV
IIMDTQYYNGKIHAYVDYPIYDVLQMVGHANRPLQDDEGRCVIMCQGSKKDFFKKFLYEP
LPVESHLDHCMHDHFNAEIVTKTIENKQDAVDYLTWTFLYRRMTQNPNYYNLQGISHRHL
SDHLSELVEQTLSDLEQSKCISIEDEMDVAPLNLGMIAAYYYINYTTIELFSMSLNAKTK
VRGLIEIISNAAEYENIPIRHHEDNLLRQLAQKVPHKLNNPKFNDPHVKTNLLLQAHLSR
MQLSAELQSDTEEILSKAIRLIQACVDVLSSNGWLSPALAAMELAQMVTQAMWSKDSYLK
QLPHFTSEHIKRCTDKGVESVFDIMEMEDEERNALLQLTDSQIADVARFCNRYPNIELSY
EVVDKDSIRSGGPVVVLVQLEREEEVTGPVIAPLFPQKREEGWWVVIGDAKSNSLISIKR
LTLQQKAKVKLDFVAPATGAHNYTLYFMSDAYMGCDQEYKFSVD

Ligands and cofactors

IDNameFormulaCopies
SANSulfanilamideC6 H8 N2 O2 S1

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:

Browse structure collections

About this viewer

MolViewer shows 4F92 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.