3N4X: Csm1 full-length

Structure of Csm1 full-length. Determined by X-ray diffraction at 3.41 Å resolution. Released 1 Sept 2010.

Method: X-ray diffraction
Resolution: 3.41 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 4,949
Mol. weight: 87.11 kDa
Released: 1 Sept 2010

Explore 3N4X in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3N4X contains 20 α-helices and 28 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: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	18-82	65
β-strand	84-86	3	1
β-strand	90-91	2	1
β-strand	96-102	7	1
β-strand	116-122	7	1
β-strand	132-134	3	1
β-strand	136	1	1
α-helix	143-152	10
α-helix	155-158	4
β-strand	161-163	3	1
α-helix	165-167	3
α-helix	168-178	11

Chain B: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	20-82	63
β-strand	85-86	2	2
β-strand	90-91	2	2
β-strand	96-101	6	2
β-strand	117-122	6	2
β-strand	132-134	3	2
β-strand	136	1	2
α-helix	143-152	10
α-helix	155-158	4
β-strand	161-163	3	2
α-helix	165-167	3
α-helix	168-178	11

Chain C: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	17-82	66
β-strand	84-86	3	3
β-strand	90-91	2	3
β-strand	96-103	8	3
β-strand	115-123	9	3
β-strand	131-134	4	3
β-strand	136	1	3
α-helix	143-152	10
α-helix	155-158	4
β-strand	161-163	3	3
α-helix	165-167	3
α-helix	168-178	11

Chain D: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	4-82	79
β-strand	84-86	3	4
β-strand	90-91	2	4
β-strand	96-102	7	4
β-strand	117-122	6	4
β-strand	132-134	3	4
β-strand	136	1	4
α-helix	143-152	10
α-helix	155-158	4
β-strand	161-163	3	4
α-helix	165-167	3
α-helix	168-178	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Monopolin complex subunit CSM1	A, B, C, D	protein	190	Saccharomyces cerevisiae	P25651 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>3N4X_1 Monopolin complex subunit CSM1 (chains A, B, C, D)
MDPLTVYKNSVKQQIDSADLLVANLVNENFVLSEKLDTKATEIKQLQKQIDSLNAQVKEL
KTQTSQQAENSEVIKDLYEYLCNVRVHKSYEDDSGLWFDISQGTHSGGSSDDYSIMDYKL
GFVKGQAQVTEVIYAPVLKQRSTEELYSLQSKLPEYLFETLSFPLSSLNQFYNKIAKSLN
KKREKKDETE

Primary citation

The Monopolin Complex Crosslinks Kinetochore Components to Regulate Chromosome-Microtubule Attachments. Corbett, K.D., Yip, C.K., Ee, L.S. et al. Cell (2010) 142:556-567. DOI 10.1016/j.cell.2010.07.017 · PubMed

Other PDB entries of the same protein (UniProt P25651 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5V3N 1.3 Å, Structure of S. cerevisiae Ulp2-Tof2-Csm1 complex
6DEI 1.7 Å, Structure of Dse3-Csm1 complex
5V1A 2.14 Å, Structure of S. cerevisiae Ulp2:Csm1 complex
3N4S 2.35 Å, Structure of Csm1 C-terminal domain, P21212 form
3N4R 2.6 Å, Structure of Csm1 C-terminal domain, R3 form
5KTB 3.05 Å, Structure of a complex between S. cerevisiae Csm1 and Mam1
3N7N 3.9 Å, Structure of Csm1/Lrs4 complex

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