3GMH: Mad2 Dimer

Crystal Structure of the Mad2 Dimer. Determined by X-ray diffraction at 3.95 Å resolution. Released 17 Nov 2010.

Method: X-ray diffraction
Resolution: 3.95 Å
Organism: Homo sapiens
Chains: 12
Atoms: 18,301
Mol. weight: 287.04 kDa
Released: 17 Nov 2010

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

Secondary structure: helices and β-sheets

3GMH contains 60 α-helices and 107 β-strands across 12 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.

Chains A and C: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	11	1	1
α-helix	13-33	21
α-helix	40-42	3
β-strand	43-48	6	2
β-strand	51-56	6	2
α-helix	59-78	20
β-strand	81-90	10	3
β-strand	96-106	11	3
β-strand	117	1	1
α-helix	121-137	17
α-helix	143-144	2
β-strand	149-157	9	3
β-strand	169	1	3
β-strand	178-187	10	3
β-strand	191-200	10	3

Chains B and D: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	11-15	5	4
α-helix	17-34	18
β-strand	43-48	6	5
β-strand	51-56	6	5
α-helix	59-76	18
β-strand	81-90	10	4
β-strand	96-106	11	4
α-helix	121-139	19
α-helix	143-145	3
β-strand	149-157	9	4
α-helix	165-167	3
β-strand	168	1	4
β-strand	173-175	3	4
β-strand	183-192	10	4
β-strand	197-199	3	6

Chains E and K: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	13-33	21
α-helix	40-42	3
β-strand	43-48	6	11
β-strand	51-56	6	11
α-helix	59-78	20
β-strand	81-90	10	12
β-strand	96-106	11	12
α-helix	121-137	17
α-helix	143-144	2
β-strand	149-157	9	12
β-strand	178-187	10	12
β-strand	191-200	10	12

Chain F: 5 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	11-15	5	13
α-helix	17-34	18
β-strand	43-48	6	14
β-strand	51-56	6	14
α-helix	59-76	18
β-strand	81-90	10	13
β-strand	96-106	11	13
α-helix	121-139	19
α-helix	143-145	3
β-strand	149-157	9	13
α-helix	165-167	3
β-strand	168	1	13
β-strand	173-175	3	13
β-strand	183-192	10	13

Chain G: 6 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	13-33	21
α-helix	40-42	3
β-strand	43-48	6	15
β-strand	51-56	6	15
α-helix	59-78	20
β-strand	81-90	10	16
β-strand	96-106	11	16
α-helix	121-137	17
α-helix	138-140	3
α-helix	143-144	2
β-strand	149-157	9	16
β-strand	169	1	17
β-strand	178-187	10	16
β-strand	191-200	10	16

Chain H: 5 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	11-15	5	18
α-helix	17-34	18
β-strand	43-48	6	5
β-strand	51-56	6	5
α-helix	59-76	18
β-strand	81-90	10	18
β-strand	96-106	11	18
α-helix	121-139	19
α-helix	143-145	3
β-strand	149-157	9	18
α-helix	165-167	3
β-strand	173-175	3	18
β-strand	183-192	10	18
β-strand	197-199	3	19

Chain I: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	13-36	24
α-helix	40-42	3
β-strand	43-48	6	20
β-strand	51-56	6	20
α-helix	59-78	20
β-strand	81-90	10	19
β-strand	96-106	11	19
α-helix	121-141	21
β-strand	149-157	9	19
β-strand	169	1	19
β-strand	178-187	10	19
β-strand	191-200	10	19

Chain J: 5 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	11-15	5	21
α-helix	17-34	18
β-strand	43-48	6	22
β-strand	51-56	6	22
α-helix	59-76	18
β-strand	81-90	10	21
β-strand	96-106	11	21
α-helix	121-139	19
α-helix	143-145	3
β-strand	149-157	9	21
α-helix	165-167	3
β-strand	168	1	21
β-strand	173-175	3	21
β-strand	183-192	10	21
β-strand	197-198	2	16
β-strand	199	1	17

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitotic spindle assembly checkpoint protein MAD2A	A, B, C, D, E, F, G, H, I, J, K, L	protein	207	Homo sapiens	Q13257 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L), FASTA

>3GMH_1 Mitotic spindle assembly checkpoint protein MAD2A (chains A, B, C, D, E, F, G, H, I, J, K, L)
MRGSHHHHHHGSITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLVTTD
LELIKYLNNVVEQLKDWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKTAKDDSAPRE
KSQKAIQDEIRSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGPQFITNS
EEVRLRSFTTTIHKVNSMVAYKIPVND

Primary citation

Structure of an intermediate conformer of the spindle checkpoint protein Mad2. Hara, M., Ozkan, E., Sun, H. et al. Proc Natl Acad Sci U S A (2015) 112:11252-11257. DOI 10.1073/pnas.1512197112 · 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…
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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