5Y5W: Human Spindlin1
Crystal structure of human Spindlin1 in complex with a histone H4K20(me3) peptide. Determined by X-ray diffraction at 3.3 Å resolution. Released 11 Oct 2017.
- Method
- X-ray diffraction
- Resolution
- 3.3 Å
- Organism
- Homo sapiens
- Chains
- 7
- Atoms
- 6,354
- Mol. weight
- 111.18 kDa
- Released
- 11 Oct 2017
Explore 5Y5W in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5Y5W contains 15 α-helices and 81 β-strands across 6 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: 3 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 42-44 | 3 | |
| β-strand | 46 | 1 | 1 |
| β-strand | 57-63 | 7 | 2 |
| β-strand | 69-79 | 11 | 2 |
| β-strand | 87-91 | 5 | 2 |
| β-strand | 96 | 1 | 3 |
| β-strand | 98-100 | 3 | 2 |
| β-strand | 108-114 | 7 | 2 |
| β-strand | 117 | 1 | 4 |
| α-helix | 126-129 | 4 | |
| β-strand | 136-142 | 7 | 3 |
| β-strand | 148-158 | 11 | 3 |
| β-strand | 166-170 | 5 | 3 |
| β-strand | 173-174 | 2 | 3 |
| β-strand | 175 | 1 | 5 |
| β-strand | 176-179 | 4 | 3 |
| α-helix | 181-186 | 6 | |
| β-strand | 190-193 | 4 | 3 |
| β-strand | 217-221 | 5 | 5 |
| β-strand | 227-235 | 9 | 5 |
| β-strand | 242-247 | 6 | 5 |
| β-strand | 252 | 1 | 2 |
| β-strand | 254-257 | 4 | 5 |
Chain B: 4 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 42-44 | 3 | |
| β-strand | 45-46 | 2 | 6 |
| β-strand | 57-62 | 6 | 7 |
| β-strand | 71-79 | 9 | 7 |
| β-strand | 87-91 | 5 | 7 |
| β-strand | 96 | 1 | 8 |
| β-strand | 98-100 | 3 | 7 |
| β-strand | 108-113 | 6 | 7 |
| α-helix | 127-131 | 5 | |
| β-strand | 136-139 | 4 | 8 |
| β-strand | 142 | 1 | 9 |
| β-strand | 148 | 1 | 9 |
| β-strand | 151-158 | 8 | 8 |
| β-strand | 166-170 | 5 | 8 |
| β-strand | 173-179 | 7 | 8 |
| α-helix | 181-186 | 6 | |
| β-strand | 190-193 | 4 | 8 |
| β-strand | 217-221 | 5 | 4 |
| α-helix | 226 | 1 | |
| β-strand | 227-235 | 9 | 4 |
| β-strand | 242-247 | 6 | 4 |
| β-strand | 252 | 1 | 7 |
| β-strand | 253-257 | 5 | 4 |
Chain C: 3 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 45-46 | 2 | 4 |
| β-strand | 57-62 | 6 | 10 |
| β-strand | 70-79 | 10 | 10 |
| β-strand | 87-91 | 5 | 10 |
| β-strand | 96 | 1 | 11 |
| β-strand | 97-100 | 4 | 10 |
| β-strand | 108-114 | 7 | 10 |
| β-strand | 117 | 1 | 1 |
| α-helix | 126-132 | 7 | |
| β-strand | 136-142 | 7 | 11 |
| β-strand | 148-158 | 11 | 11 |
| β-strand | 166-170 | 5 | 11 |
| β-strand | 173-174 | 2 | 11 |
| β-strand | 175 | 1 | 6 |
| β-strand | 176-179 | 4 | 11 |
| α-helix | 181-186 | 6 | |
| β-strand | 190 | 1 | 11 |
| β-strand | 217-221 | 5 | 6 |
| β-strand | 227-235 | 9 | 6 |
| β-strand | 242-247 | 6 | 6 |
| β-strand | 252 | 1 | 10 |
| α-helix | 253 | 1 | |
| β-strand | 254-257 | 4 | 6 |
Chain D: 2 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 57-59 | 3 | 12 |
| β-strand | 62 | 1 | 13 |
| β-strand | 70 | 1 | 13 |
| β-strand | 73-79 | 7 | 12 |
| β-strand | 87-91 | 5 | 12 |
| β-strand | 96 | 1 | 14 |
| β-strand | 98-100 | 3 | 12 |
| β-strand | 108 | 1 | 13 |
| β-strand | 112 | 1 | 12 |
| α-helix | 129-132 | 4 | |
| β-strand | 136-141 | 6 | 14 |
| β-strand | 149-158 | 10 | 14 |
| β-strand | 166-170 | 5 | 14 |
| β-strand | 175 | 1 | 15 |
| β-strand | 177-179 | 3 | 14 |
| α-helix | 181-185 | 5 | |
| β-strand | 190-193 | 4 | 14 |
| β-strand | 217-222 | 6 | 15 |
| β-strand | 226-235 | 10 | 15 |
| β-strand | 242-247 | 6 | 15 |
| β-strand | 252 | 1 | 12 |
| β-strand | 254-257 | 4 | 15 |
Chain E: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-19 | 2 | 3 |
| α-helix | 20 | 1 | |
Chain G: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 18 | 1 | |
| β-strand | 19 | 1 | 11 |
| α-helix | 20 | 1 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Spindlin-1 | A, B, C, D | protein | 235 | Homo sapiens | Q9Y657 (AlphaFold model) |
| Histone peptide H4K20(me3) | E, F, G | protein | 9 | Homo sapiens | |
Sequence of entity 1 (A, B, C, D), FASTA
>5Y5W_1 Spindlin-1 (chains A, B, C, D)
MSSGHHHHHHHHGSSENLYFQGSRNIVGCRIQHGWKEGNGPVTQWKGTVLDQVPVNPSLY
LIKYDGFDCVYGLELNKDERVSALEVLPDRVATSRISDAHLADTMIGKAVEHMFETEDGS
KDEWRGMVLARAPVMNTWFYITYEKDPVLYMYQLLDDYKEGDLRIMPDSNDSPPAEREPG
EVVDSLVGKQVEYAKEDGSKRTGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKTS
Sequence of entity 2 (E, F, G), FASTA
>5Y5W_2 Histone peptide H4K20(me3) (chains E, F, G)
KRHRKVLDN
Primary citation
Spindlin-1 recognizes methylations of K20 and R23 of histone H4 tail. Wang, C., Zhan, L., Wu, M. et al. FEBS Lett (2018) 592:4098-4110. DOI 10.1002/1873-3468.13281 · PubMed
Other PDB entries of the same protein (UniProt Q9Y657 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7OCB 1.42 Å, Crystal structure of Spindlin1 in complex with the inhibitor XY49-92B
- 6I8Y 1.52 Å, Crystal structure of Spindlin1 in complex with the Methyltransferase inhibitor A366
- 6I8L 1.58 Å, Crystal structure of Spindlin1 in complex with the inhibitor TD001851a
- 6QPL 1.6 Å, Crystal structure of Spindlin1 in complex with the inhibitor MS31
- 7CNA 1.6 Å, Crystal structure of Spindlin1/C11orf84 complex bound to histone H3K4me3K9me3 peptide
- 4MZG 1.7 Å, Crystal structure of human Spindlin1 bound to histone H3K4me3 peptide
- 6I8B 1.76 Å, Crystal structure of Spindlin1 in complex with the inhibitor VinSpinIn
- 8GTX 1.8 Å, Crystal Structure of human Spindlin1-HBx complex
- 9T2Z 1.87 Å, Spindlin 1 with crystallization epitope mutations H127D:L128D:T131R
- 4H75 2.1 Å, Crystal structure of human Spindlin1 in complex with a histone H3K4(me3) peptide
- 4MZF 2.1 Å, Crystal structure of human Spindlin1 bound to histone H3(K4me3-R8me2a) peptide
- 2NS2 2.2 Å, Crystal Structure of Spindlin1
Browse structure collections
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