2I3S: Bub3 complex with Bub1 GLEBS motif

Bub3 complex with Bub1 GLEBS motif. Determined by X-ray diffraction at 1.9 Å resolution. Released 9 Jan 2007.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Saccharomyces cerevisiae
Chains
6
Atoms
9,442
Mol. weight
131.71 kDa
Released
9 Jan 2007

Explore 2I3S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2I3S contains 29 α-helices and 99 β-strands across 6 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: 9 helices, 32 β-strands

ElementResiduesLengthSheet
β-strand2-541
α-helix131
β-strand14-2072
α-helix21-233
β-strand25-3062
β-strand34-4182
β-strand46-5492
β-strand59-6683
β-strand70-7673
β-strand81-8443
β-strand92-9433
α-helix951
β-strand9614
β-strand104-11075
β-strand114-11965
β-strand123-12755
α-helix129-1324
β-strand13514
β-strand136-14165
β-strand153-15866
β-strand162-16766
β-strand171-17666
β-strand186-18946
β-strand196-20167
α-helix204-2063
β-strand208-21367
β-strand217-22267
β-strand236-23947
β-strand242-24328
β-strand249-25138
β-strand254-25969
α-helix2651
β-strand266-27059
β-strand275-27959
β-strand284-28859
α-helix289-2913
β-strand296-30271
β-strand306-31271
α-helix315-3184
α-helix328-3314
β-strand332-33761
Chains B, D and F: 2 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand317-31938
α-helix323-3264
α-helix336-3438
Chain C: 6 helices, 32 β-strands
ElementResiduesLengthSheet
β-strand2-5410
β-strand14-20711
β-strand25-30611
β-strand34-41811
β-strand46-54911
β-strand59-66812
β-strand70-76712
β-strand81-84412
β-strand92-94312
α-helix951
β-strand96113
β-strand104-110714
β-strand114-119614
β-strand123-127514
β-strand135113
β-strand140-141214
β-strand153-158615
β-strand162-167615
β-strand171-176615
β-strand186-189415
β-strand196-201616
α-helix202-2032
α-helix204-2063
β-strand208-213616
β-strand217-222616
β-strand236-239416
β-strand242-243217
β-strand249-251317
β-strand254-259618
β-strand266-270518
β-strand275-279518
β-strand284-288518
α-helix289-2913
β-strand296-302710
β-strand306-312710
α-helix315-3184
α-helix328-3314
β-strand332-337610
Chain E: 8 helices, 32 β-strands
ElementResiduesLengthSheet
β-strand2-5419
α-helix131
β-strand14-20720
α-helix21-233
β-strand25-30620
β-strand34-41820
β-strand46-54920
β-strand59-65721
β-strand71-76621
β-strand81-84421
β-strand92-94321
α-helix951
β-strand96122
β-strand104-110723
β-strand114-119623
β-strand123-127523
β-strand135122
β-strand140-141223
β-strand153-159724
β-strand162-167624
α-helix168-1703
β-strand171-176624
β-strand186-189424
β-strand196-201625
α-helix204-2063
β-strand208-213625
β-strand217-222625
β-strand236-239425
β-strand242-243226
β-strand249-251326
β-strand256-259427
β-strand266-269427
β-strand275-279527
β-strand284-288527
α-helix289-2913
β-strand296-302719
β-strand306-312719
α-helix315-3184
α-helix329-3313
β-strand332-337619

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cell cycle arrest proteinA, C, Eprotein349Saccharomyces cerevisiaeP26449 (AlphaFold model)
Checkpoint serine/threonine-protein kinaseB, D, Fprotein36Saccharomyces cerevisiaeP41695 (AlphaFold model)
Sequence of entity 1 (A, C, E), FASTA
>2I3S_1 Cell cycle arrest protein (chains A, C, E)
MQIVQIEQAPKDYISDIKIIPSKSLLLITSWDGSLTVYKFDIQAKNVDLLQSLRYKHPLL
CCNFIDNTDLQIYVGTVQGEILKVDLIGSPSFQALTNNEANLGICRICKYGDDKLIAASW
DGLIEVIDPRNYGDGVIAVKNLNSNNTKVKNKIFTMDTNSSRLIVGMNNSQVQWFRLPLC
EDDNGTIEESGLKYQIRDVALLPKEQEGYACSSIDGRVAVEFFDDQGDDYNSSKRFAFRC
HRLNLKDTNLAYPVNSIEFSPRHKFLYTAGSDGIISCWNLQTRKKIKNFAKFNEDSVVKI
ACSDNILCLATSDDTFKTNAAIDQTIELNASSIYIIFDYENELHHHHHH
Sequence of entity 2 (B, D, F), FASTA
>2I3S_2 Checkpoint serine/threonine-protein kinase (chains B, D, F)
KPERIVFNFNLIYPENDEEFNTEEILAMIKGLYKVQ

Primary citation

Structural analysis of Bub3 interactions in the mitotic spindle checkpoint. Larsen, N.A., Al-Bassam, J., Wei, R.R. et al. Proc Natl Acad Sci U S A (2007) 104:1201-1206. DOI 10.1073/pnas.0610358104 · PubMed

Other PDB entries of the same protein (UniProt P26449 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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