4E45: HMHF1/hMHF2 Histone-Fold Tetramer
Crystal structure of the hMHF1/hMHF2 Histone-Fold Tetramer in Complex with Fanconi Anemia Associated Helicase hFANCM. Determined by X-ray diffraction at 2.0 Å resolution. Released 20 Mar 2013.
- Method
- X-ray diffraction
- Resolution
- 2.0 Å
- Organism
- Homo sapiens
- Chains
- 15
- Atoms
- 11,040
- Mol. weight
- 182.34 kDa
- Ligands
- ZN
- Released
- 20 Mar 2013
Explore 4E45 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4E45 contains 78 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 | 5-38 | 34 | |
| β-strand | 41-42 | 2 | 1 |
| α-helix | 44-71 | 28 | |
| β-strand | 76-77 | 2 | 2 |
| α-helix | 79-84 | 6 | |
| α-helix | 90-104 | 15 | |
Chains B, D and N: 3 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-22 | 11 | |
| β-strand | 29-30 | 2 | 2 |
| α-helix | 32-59 | 28 | |
| β-strand | 64-65 | 2 | 1 |
| α-helix | 67-80 | 14 | |
Chain C: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-38 | 24 | |
| β-strand | 41-42 | 2 | 3 |
| α-helix | 44-71 | 28 | |
| β-strand | 76-77 | 2 | 4 |
| α-helix | 79-85 | 7 | |
| α-helix | 90-104 | 15 | |
Chain E: 12 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 680-681 | 2 | |
| α-helix | 682-687 | 6 | |
| α-helix | 688-692 | 5 | |
| β-strand | 702-704 | 3 | 5 |
| α-helix | 706-708 | 3 | |
| β-strand | 728-730 | 3 | 5 |
| α-helix | 731-732 | 2 | |
| α-helix | 737-739 | 3 | |
| α-helix | 743-745 | 3 | |
| α-helix | 750-752 | 3 | |
| α-helix | 753-768 | 16 | |
| α-helix | 776-781 | 6 | |
| α-helix | 782-784 | 3 | |
| α-helix | 787-789 | 3 | |
Chain F: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-38 | 34 | |
| β-strand | 42 | 1 | 6 |
| α-helix | 44-71 | 28 | |
| β-strand | 76-77 | 2 | 7 |
| α-helix | 79-85 | 7 | |
| α-helix | 90-104 | 15 | |
Chains G and L: 3 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-22 | 11 | |
| β-strand | 29-30 | 2 | 7 |
| α-helix | 32-59 | 28 | |
| β-strand | 65 | 1 | 6 |
| α-helix | 67-80 | 14 | |
Chain H: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-37 | 23 | |
| β-strand | 41-42 | 2 | 8 |
| α-helix | 44-71 | 28 | |
| β-strand | 76-77 | 2 | 9 |
| α-helix | 79-85 | 7 | |
| α-helix | 90-103 | 14 | |
Chain I: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-22 | 11 | |
| β-strand | 29-30 | 2 | 9 |
| α-helix | 32-59 | 28 | |
| β-strand | 64-65 | 2 | 8 |
| α-helix | 67-72 | 6 | |
| α-helix | 74-79 | 6 | |
4 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, C, F, H, K, M | protein | 112 | Homo sapiens | Q8N2Z9 (AlphaFold model) |
| Centromere protein X | B, D, G, I, L, N | protein | 83 | Homo sapiens | A8MT69 (AlphaFold model) |
| Fanconi anemia group M protein | E, J, O | protein | 137 | Homo sapiens | Q8IYD8 (AlphaFold model) |
Sequence of entity 1 (A, C, F, H, K, M), FASTA
>4E45_1 Centromere protein S (chains A, C, F, H, K, M)
GSMEEEAETEEQQRFSYQQRLKAAVHYTVGCLCEEVALDKEMQFSKQTIAAISELTFRQC
ENFAKDLEMFARHAKRTTINTEDVKLLARRSNSLLKYITDKSEEIAQINLER
Sequence of entity 2 (B, D, G, I, L, N), FASTA
>4E45_2 Centromere protein X (chains B, D, G, I, L, N)
GSMEGAGAGSGFRKELVSRLLHLHFKDDKTKVSGDALQLMVELLKVFVVEAAVRGVRQAQ
AEDALRVDVDQLEKVLPQLLLDF
Sequence of entity 3 (E, J, O), FASTA
>4E45_3 Fanconi anemia group M protein (chains E, J, O)
GAMDPMRQSSLKKDWFLSEEEFKLWNRLYRLRDSDEIKEITLPQVQFSSLQNEENKPAQE
STTGIHQLSLSEWRLWQDHPLPTHQVDHSDRCRHFIGLMQMIEGMRHEEGECSYELEVES
YLQMEDVTSTFIAPRNE
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 3 |
Water and common crystallization additives (GOL) are not listed.
Primary citation
Crystal Structures Reveal that FANCM remodels the MHF Tetramer in favor of binding Branched DNA. Fox III, D., Yan, Z., Ling, C. et al. To be published.
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
- 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
- 4DRB 2.63 Å, The crystal structure of FANCM bound MHF 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
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