1GO4: PDB entry 1GO4

Crystal structure of Mad1-Mad2 reveals a conserved Mad2 binding motif in Mad1 and Cdc20. Determined by X-ray diffraction at 2.05 Å resolution. Released 16 May 2002.

Method: X-ray diffraction
Resolution: 2.05 Å
Organism: Homo sapiens
Chains: 8
Atoms: 9,928
Mol. weight: 140.56 kDa
Released: 16 May 2002

Explore 1GO4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1GO4 contains 37 α-helices and 48 β-strands across 8 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: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	11	1	1
α-helix	13-34	22
α-helix	40-42	3
β-strand	43-48	6	2
β-strand	51-56	6	2
α-helix	59-77	19
β-strand	81-90	10	3
β-strand	96-106	11	3
α-helix	108-111	4
β-strand	117	1	1
α-helix	121-137	17
α-helix	138-140	3
α-helix	143-145	3
β-strand	149-158	10	3
β-strand	167-169	3	3
β-strand	176	1	4
β-strand	179-182	4	3
β-strand	186-187	2	3
β-strand	191-199	9	3

Chain B: 8 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	11	1	5
α-helix	13-34	22
α-helix	40-42	3
β-strand	43-48	6	6
β-strand	51-56	6	6
α-helix	59-78	20
β-strand	81-90	10	7
β-strand	96-106	11	7
α-helix	108-112	5
β-strand	117	1	5
α-helix	121-139	19
α-helix	143-145	3
β-strand	149-158	10	7
α-helix	161-164	4
β-strand	167-169	3	7
β-strand	178-187	10	7
β-strand	191-200	10	7
α-helix	201-202	2

Chain C: 8 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	11	1	8
α-helix	13-34	22
α-helix	40-42	3
β-strand	43-48	6	9
β-strand	51-56	6	9
α-helix	59-77	19
β-strand	81-90	10	10
β-strand	96-106	11	10
α-helix	108-112	5
β-strand	117	1	8
α-helix	121-137	17
α-helix	138-140	3
α-helix	143-145	3
β-strand	149-158	10	10
α-helix	161-164	4
β-strand	167-169	3	10
β-strand	178-182	5	10
β-strand	186-187	2	10
β-strand	191-200	10	10

Chain D: 6 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	13-35	23
α-helix	40-42	3
β-strand	43-48	6	11
β-strand	51-56	6	11
α-helix	61-77	17
β-strand	81-90	10	12
β-strand	96-106	11	12
α-helix	108-112	5
α-helix	121-137	17
β-strand	149-158	10	12
β-strand	167-169	3	12
β-strand	178-187	10	12
β-strand	191-200	10	12
α-helix	201-202	2

Chain E: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	494-528	35
β-strand	540-545	6	10
α-helix	549-575	27

Chain F: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	499-532	34
β-strand	540-545	6	7
α-helix	549-577	29

Chain G: 2 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	487-527	41
β-strand	529	1	13
β-strand	531	1	4
β-strand	540-545	6	3
α-helix	549-578	30

Chain H: 2 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	494-530	37
β-strand	536	1	13
β-strand	540-545	6	12
α-helix	549-577	29

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitotic spindle assembly checkpoint protein MAD2A	A, B, C, D	protein	205	Homo sapiens	Q13257 (AlphaFold model)
Mitotic spindle assembly checkpoint protein MAD1	E, F, G, H	protein	100	Homo sapiens	Q9Y6D9 (AlphaFold model)

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

>1GO4_1 Mitotic spindle assembly checkpoint protein MAD2A (chains A, B, C, D)
MALQLSREQGITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLVTTDLE
LIKYLNNVVEQLKDWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKTAKDDSAPREKS
QKAIQDEIRSVIAQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGPQFITNSEE
VRLRSFTTTIHKVNSMVAYKIPVND

Sequence of entity 2 (E, F, G, H), FASTA

>1GO4_2 Mitotic spindle assembly checkpoint protein MAD1 (chains E, F, G, H)
SSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLH
MSLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTV

Primary citation

Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint. Sironi, L., Mapelli, M., Knapp, S. et al. EMBO J (2002) 21:2496-2506. DOI 10.1093/emboj/21.10.2496 · 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
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
1KLQ The Mad2 Spindle Checkpoint Protein Undergoes Similar Major Conformational Changes upon…
1S2H The Mad2 spindle checkpoint protein possesses two distinct natively folded states

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