1KLQ: PDB entry 1KLQ

The Mad2 Spindle Checkpoint Protein Undergoes Similar Major Conformational Changes upon Binding to Either Mad1 or Cdc20. Determined by solution NMR. Released 25 Jan 2002.

Method: Solution NMR
Organism: Homo sapiens
Chains: 2
Atoms: 1,680
Mol. weight: 24.01 kDa
Released: 25 Jan 2002

Explore 1KLQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KLQ contains 5 α-helices and 9 β-strands across 2 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, 8 β-strands

Element	Residues	Length	Sheet
α-helix	15-37	23
α-helix	42-44	3
β-strand	45-50	6	1
β-strand	53-58	6	1
α-helix	61-73	13
α-helix	74-78	5
β-strand	85-92	8	2
β-strand	97-108	12	2
α-helix	124-143	20
β-strand	151-158	8	2
β-strand	172	1	2
β-strand	180-189	10	2
β-strand	193-202	10	2

Chain B: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	2-5	4	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitotic spindle assembly checkpoint protein MAD2A	A	protein	197	Homo sapiens	Q13257 (AlphaFold model)
Mad2-binding peptide	B	protein	12

Sequence of entity 1 (A), FASTA

>1KLQ_1 MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A (chains A)
GSITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLVTTDLELIKYLNNV
VEQLKDWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKTAKDDSAPREKSQKAIQDEI
RSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGPQFITNSEEVRLRSFTT
TIHKVNSMVAYKIPVND

Sequence of entity 2 (B), FASTA

>1KLQ_2 Mad2-binding peptide (chains B)
SWYSYPPPQRAV

Primary citation

The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20. Luo, X., Tang, Z., Rizo, J. et al. Mol Cell (2002) 9:59-71. DOI 10.1016/S1097-2765(01)00435-X · PubMed

Other PDB entries of the same protein (UniProt Q13257 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2VFX 1.95 Å, Structure of the Symmetric Mad2 Dimer
1GO4 2.05 Å, Crystal structure of Mad1-Mad2 reveals a conserved Mad2 binding motif in Mad1 and Cdc20.
2QYF 2.3 Å, Crystal structure of the Mad2/p31(comet)/Mad2-binding peptide ternary complex
2V64 2.9 Å, Crystallographic structure of the conformational dimer of the Spindle Assembly…
6TLJ 3.8 Å, Cryo-EM structure of the Anaphase-promoting complex/Cyclosome, in complex with the…
3GMH 3.95 Å, Crystal Structure of the Mad2 Dimer
5LCW 4.2 Å, Cryo-EM structure of the Anaphase-promoting complex/Cyclosome, in complex with the…
6F0X 4.6 Å, Cryo-EM structure of TRIP13 in complex with ATP gamma S, p31comet, C-Mad2 and Cdc20
5KHU 4.8 Å, Model of human Anaphase-promoting complex/Cyclosome (APC15 deletion mutant), in complex…
1DUJ Solution structure of the spindle assembly checkpoint protein human MAD2
1S2H The Mad2 spindle checkpoint protein possesses two distinct natively folded states

Browse structure collections

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