2V64: PDB entry 2V64
Crystallographic structure of the conformational dimer of the Spindle Assembly Checkpoint protein Mad2. Determined by X-ray diffraction at 2.9 Å resolution. Released 27 Nov 2007.
- Method
- X-ray diffraction
- Resolution
- 2.9 Å
- Organisms
- HOMO SAPIENS, SYNTHETIC CONSTRUCT
- Chains
- 9
- Atoms
- 9,648
- Mol. weight
- 149.17 kDa
- Released
- 27 Nov 2007
Explore 2V64 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2V64 contains 41 α-helices and 57 β-strands across 9 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 F: 8 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-8 | 7 | |
| 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 | 108-112 | 5 | |
| β-strand | 117 | 1 | 1 |
| α-helix | 121-137 | 17 | |
| α-helix | 138-140 | 3 | |
| α-helix | 143-144 | 2 | |
| β-strand | 149-157 | 9 | 3 |
| β-strand | 168-170 | 3 | 3 |
| β-strand | 178-187 | 10 | 3 |
| β-strand | 191-200 | 10 | 3 |
Chains B and G: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 3 |
| α-helix | 6-8 | 3 | |
Chain C: 7 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-8 | 7 | |
| β-strand | 11 | 1 | 4 |
| α-helix | 13-34 | 22 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-48 | 6 | 5 |
| β-strand | 51-56 | 6 | 5 |
| α-helix | 59-77 | 19 | |
| β-strand | 81-90 | 10 | 6 |
| β-strand | 96-106 | 11 | 6 |
| α-helix | 110-112 | 3 | |
| β-strand | 117 | 1 | 4 |
| α-helix | 121-137 | 17 | |
| α-helix | 143-144 | 2 | |
| β-strand | 149-157 | 9 | 6 |
| β-strand | 168-170 | 3 | 6 |
| β-strand | 178-187 | 10 | 6 |
| β-strand | 191-200 | 10 | 6 |
Chains D and H: 5 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 11-15 | 5 | 7 |
| α-helix | 17-34 | 18 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-48 | 6 | 8 |
| β-strand | 51-56 | 6 | 8 |
| α-helix | 59-76 | 18 | |
| β-strand | 81-90 | 10 | 7 |
| β-strand | 96-106 | 11 | 7 |
| α-helix | 121-139 | 19 | |
| α-helix | 143-145 | 3 | |
| β-strand | 149-157 | 9 | 7 |
| β-strand | 173-175 | 3 | 7 |
| β-strand | 183-192 | 10 | 7 |
Chain E: 5 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 11-14 | 4 | 9 |
| α-helix | 17-34 | 18 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-48 | 6 | 10 |
| β-strand | 51-56 | 6 | 10 |
| α-helix | 59-76 | 18 | |
| β-strand | 81-90 | 10 | 9 |
| β-strand | 96-105 | 10 | 9 |
| α-helix | 121-139 | 19 | |
| α-helix | 143-145 | 3 | |
| β-strand | 149-157 | 9 | 9 |
| β-strand | 173-175 | 3 | 9 |
| β-strand | 183-192 | 10 | 9 |
Chain I: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-5 | 4 | 6 |
| α-helix | 6-8 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Mitotic spindle assembly checkpoint protein MAD2A | A, C, F | protein | 213 | HOMO SAPIENS | Q13257 (AlphaFold model) |
| MBP1 | B, G, I | protein | 12 | SYNTHETIC CONSTRUCT | |
| Mitotic spindle assembly checkpoint protein MAD2A | D, E, H | protein | 207 | HOMO SAPIENS | Q13257 (AlphaFold model) |
Sequence of entity 1 (A, C, F), FASTA
>2V64_1 MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A (chains A, C, F)
MHHHHHHGSALQLSREQGITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLT
LLVTTDLELIKYLNNVVEQLKDWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKTAKD
DSAPREKSQKAIQDEIRSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGP
QFITNSEEVRLRSFTTTIHKVNSMVAYKIPVND
Sequence of entity 2 (B, G, I), FASTA
>2V64_2 MBP1 (chains B, G, I)
SWYSYPPPQRAV
Sequence of entity 3 (D, E, H), FASTA
>2V64_3 MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A (chains D, E, H)
MHHHHHHGSALQLSREQGITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLT
LLVTTDLELIKYLNNVVEQLKDWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKGSGE
KSQKAIQDEIRSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGPQFITNS
EEVRLRSFTTTIHKVNSMVAYKIPVND
Primary citation
The MAD2 Conformational Dimer: Structure and Implications for the Spindle Assembly Checkpoint. Mapelli, M., Massimiliano, L., Santaguida, S. et al. Cell (2007) 131:730. DOI 10.1016/J.CELL.2007.08.049 · 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
- 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
Browse structure collections
About this viewer
MolViewer shows 2V64 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.