4DRB: FANCM bound MHF complex
The crystal structure of FANCM bound MHF complex. Determined by X-ray diffraction at 2.63 Å resolution. Released 16 May 2012.
- Method
- X-ray diffraction
- Resolution
- 2.63 Å
- Organism
- Homo sapiens
- Chains
- 15
- Atoms
- 10,508
- Mol. weight
- 192.58 kDa
- Released
- 16 May 2012
Explore 4DRB in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4DRB contains 74 α-helices and 30 β-strands across 15 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: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-38 | 24 | |
| β-strand | 41-42 | 2 | 1 |
| α-helix | 44-71 | 28 | |
| β-strand | 76-77 | 2 | 2 |
| α-helix | 79-85 | 7 | |
| α-helix | 90-107 | 18 | |
Chain B: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-38 | 33 | |
| β-strand | 42 | 1 | 3 |
| α-helix | 44-71 | 28 | |
| β-strand | 76-77 | 2 | 4 |
| α-helix | 79-84 | 6 | |
| α-helix | 90-106 | 17 | |
Chain C: 6 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 682-691 | 10 | |
| β-strand | 702-704 | 3 | 5 |
| β-strand | 728-730 | 3 | 5 |
| α-helix | 737-739 | 3 | |
| α-helix | 743-745 | 3 | |
| α-helix | 753-767 | 15 | |
| α-helix | 776-782 | 7 | |
| α-helix | 787-789 | 3 | |
Chain D: 5 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-12 | 3 | |
| α-helix | 15-37 | 23 | |
| β-strand | 41-42 | 2 | 6 |
| α-helix | 44-71 | 28 | |
| β-strand | 76-77 | 2 | 7 |
| α-helix | 79-85 | 7 | |
| α-helix | 90-104 | 15 | |
Chain E: 5 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-38 | 28 | |
| β-strand | 42 | 1 | 8 |
| α-helix | 44-71 | 28 | |
| β-strand | 76-77 | 2 | 9 |
| α-helix | 79-83 | 5 | |
| α-helix | 84-86 | 3 | |
| α-helix | 90-102 | 13 | |
Chain F: 8 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 682-691 | 10 | |
| α-helix | 693-695 | 3 | |
| β-strand | 702-704 | 3 | 10 |
| β-strand | 728-730 | 3 | 10 |
| α-helix | 737-739 | 3 | |
| α-helix | 743-745 | 3 | |
| α-helix | 750-752 | 3 | |
| α-helix | 753-766 | 14 | |
| α-helix | 776-781 | 6 | |
| α-helix | 782-784 | 3 | |
Chain G: 5 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-37 | 33 | |
| β-strand | 41-42 | 2 | 11 |
| α-helix | 44-71 | 28 | |
| β-strand | 76-77 | 2 | 12 |
| α-helix | 79-83 | 5 | |
| α-helix | 84-86 | 3 | |
| α-helix | 90-106 | 17 | |
Chain H: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-37 | 23 | |
| β-strand | 41-42 | 2 | 13 |
| α-helix | 44-71 | 28 | |
| β-strand | 76-77 | 2 | 14 |
| α-helix | 79-85 | 7 | |
| α-helix | 90-105 | 16 | |
6 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 |
|---|
| Centromere protein S | A, B, D, E, G, H | protein | 120 | Homo sapiens | Q8N2Z9 (AlphaFold model) |
| Fanconi anemia group M protein | C, F, I | protein | 141 | Homo sapiens | Q8IYD8 (AlphaFold model) |
| Centromere protein X | J, K, L, M, N, O | protein | 84 | Homo sapiens | A8MT69 (AlphaFold model) |
Sequence of entity 1 (A, B, D, E, G, H), FASTA
>4DRB_1 Centromere protein S (chains A, B, D, E, G, H)
HHHHHHMEEEAETEEQQRFSYQQRLKAAVHYTVGCLCEEVALDKEMQFSKQTIAAISELT
FRQCENFAKDLEMFARHAKRTTINTEDVKLLARRSNSLLKYITDKSEEIAQINLERKAQK
Sequence of entity 2 (C, F, I), FASTA
>4DRB_2 Fanconi anemia group M protein (chains C, F, I)
GSIFSYRDGMRQSSLKKDWFLSEEEFKLWNRLYRLRDSDEIKEITLPQVQFSSLQNEENK
PAQESTTGIHQLSLSEWRLWQDHPLPTHQVDHSDRCRHFIGLMQMIEGMRHEEGECSYEL
EVESYLQMEDVTSTFIAPRNE
Sequence of entity 3 (J, K, L, M, N, O), FASTA
>4DRB_3 Centromere protein X (chains J, K, L, M, N, O)
GSHMEGAGAGSGFRKELVSRLLHLHFKDDKTKVSGDALQLMVELLKVFVVEAAVRGVRQA
QAEDALRVDVDQLEKVLPQLLLDF
Primary citation
The structure of the FANCM-MHF complex reveals physical features for functional assembly. Tao, Y., Jin, C., Li, X. et al. Nat Commun (2012) 3:782-782. DOI 10.1038/ncomms1779 · PubMed
Other PDB entries of the same protein (UniProt Q8N2Z9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4NE3 1.8 Å, Human MHF1-MHF2 complex
- 4E45 2.0 Å, Crystal structure of the hMHF1/hMHF2 Histone-Fold Tetramer in Complex with Fanconi…
- 4E44 2.1 Å, Crystal structure of the hMHF1/hMHF2 Histone-Fold Tetramer
- 4NE6 2.1 Å, Human MHF1-MHF2 complex
- 4DRA 2.41 Å, Crystal structure of MHF complex
- 4NE5 2.5 Å, Human MHF1-MHF2 complex
- 28OP 2.7 Å, Structure of the human inner kinetochore CCAN and CENP-C bound to DNA
- 7R5S 2.83 Å, Structure of the human CCAN bound to alpha satellite DNA
- 7XHO 3.29 Å, Structure of human inner kinetochore CCAN complex
- 9TAW 3.54 Å, Structure of the human inner kinetochore CCAN bound to DNA
- 7XHN 3.71 Å, Structure of human inner kinetochore CCAN-DNA complex
- 9TAX 4.5 Å, Structure of the human inner kinetochore CCAN bound to a mono-CENP-A nucleosome
Browse structure collections
About this viewer
MolViewer shows 4DRB 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.