6BX3: Histone H3k4 methyltransferase
Structure of histone H3k4 methyltransferase. Determined by electron microscopy at 4.3 Å resolution. Released 5 Sept 2018.
- Method
- Electron microscopy
- Resolution
- 4.3 Å
- Organisms
- Saccharomyces cerevisiae (strain YJM789), Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
- Chains
- 7
- Atoms
- 10,456
- Mol. weight
- 199.98 kDa
- Released
- 5 Sept 2018
Explore 6BX3 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6BX3 contains 36 α-helices and 92 β-strands across 7 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: 5 helices, 36 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 28 | 1 | 24 |
| β-strand | 32 | 1 | 25 |
| β-strand | 35 | 1 | 25 |
| β-strand | 40 | 1 | 24 |
| β-strand | 47 | 1 | 24 |
| α-helix | 57-58 | 2 | |
| β-strand | 61-62 | 2 | 26 |
| β-strand | 69-73 | 5 | 26 |
| β-strand | 79-83 | 5 | 26 |
| β-strand | 92 | 1 | 26 |
| α-helix | 98-99 | 2 | |
| β-strand | 102-104 | 3 | 27 |
| β-strand | 110-113 | 4 | 27 |
| β-strand | 115 | 1 | 28 |
| β-strand | 120-124 | 5 | 27 |
| β-strand | 129-134 | 6 | 27 |
| β-strand | 141-143 | 3 | 28 |
| β-strand | 154 | 1 | 29 |
| β-strand | 157-158 | 2 | 28 |
| β-strand | 162-163 | 2 | 30 |
| β-strand | 166 | 1 | 29 |
| β-strand | 177-178 | 2 | 30 |
| β-strand | 195 | 1 | 31 |
| β-strand | 204-207 | 4 | 31 |
| α-helix | 208 | 1 | |
| β-strand | 213-216 | 4 | 31 |
| β-strand | 223-227 | 5 | 31 |
| β-strand | 245 | 1 | 32 |
| β-strand | 248-250 | 3 | 33 |
| β-strand | 254-257 | 4 | 33 |
| α-helix | 258 | 1 | |
| α-helix | 264-266 | 3 | |
| β-strand | 267-268 | 2 | 33 |
| β-strand | 275 | 1 | 33 |
| β-strand | 292 | 1 | 32 |
| β-strand | 295 | 1 | 34 |
| β-strand | 300 | 1 | 34 |
| β-strand | 303 | 1 | 32 |
| β-strand | 304 | 1 | 35 |
| β-strand | 308 | 1 | 35 |
| β-strand | 314 | 1 | 34 |
Chain B: 4 helices, 32 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 22-23 | 2 | 12 |
| β-strand | 29-34 | 6 | 13 |
| β-strand | 41-45 | 5 | 13 |
| β-strand | 79-80 | 2 | 14 |
| β-strand | 86-88 | 3 | 14 |
| β-strand | 95-98 | 4 | 15 |
| β-strand | 99-100 | 2 | 14 |
| β-strand | 109-112 | 4 | 15 |
| β-strand | 120-122 | 3 | 16 |
| β-strand | 130-132 | 3 | 16 |
| β-strand | 141-143 | 3 | 16 |
| β-strand | 151-152 | 2 | 16 |
| β-strand | 173-176 | 4 | 17 |
| β-strand | 184-187 | 4 | 17 |
| β-strand | 193-196 | 4 | 17 |
| β-strand | 199 | 1 | 18 |
| β-strand | 203 | 1 | 18 |
| β-strand | 206-209 | 4 | 17 |
| β-strand | 222 | 1 | 19 |
| β-strand | 228 | 1 | 20 |
| β-strand | 229 | 1 | 19 |
| β-strand | 242 | 1 | 20 |
| α-helix | 243-244 | 2 | |
| β-strand | 245 | 1 | 21 |
| β-strand | 248 | 1 | 21 |
| β-strand | 269-274 | 6 | 22 |
| β-strand | 281-286 | 6 | 22 |
| β-strand | 295 | 1 | 23 |
| β-strand | 297-298 | 2 | 22 |
| β-strand | 307 | 1 | 23 |
| β-strand | 315-320 | 6 | 12 |
| β-strand | 327-331 | 5 | 12 |
| β-strand | 337-339 | 3 | 12 |
| α-helix | 343-345 | 3 | |
| α-helix | 356-358 | 3 | |
| α-helix | 404-406 | 3 | |
Chain E: 4 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 800-823 | 24 | |
| α-helix | 926-932 | 7 | |
| β-strand | 967 | 1 | 1 |
| α-helix | 975-987 | 13 | |
| β-strand | 995 | 1 | 2 |
| β-strand | 1003 | 1 | 2 |
| β-strand | 1016 | 1 | 3 |
| β-strand | 1023-1026 | 4 | 4 |
| β-strand | 1036 | 1 | 1 |
| β-strand | 1037-1041 | 5 | 4 |
| α-helix | 1048-1050 | 3 | |
| β-strand | 1051 | 1 | 3 |
| β-strand | 1052 | 1 | 4 |
Chain F: 10 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 118-128 | 11 | |
| α-helix | 136-144 | 9 | |
| α-helix | 151-157 | 7 | |
| α-helix | 165-170 | 6 | |
| α-helix | 184-185 | 2 | |
| α-helix | 192-199 | 8 | |
| α-helix | 203-207 | 5 | |
| α-helix | 209-240 | 32 | |
| α-helix | 279-282 | 4 | |
| α-helix | 312-348 | 37 | |
Chain K: 8 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 99-101 | 3 | |
| α-helix | 103-105 | 3 | |
| α-helix | 121-124 | 4 | |
| β-strand | 128 | 1 | 5 |
| β-strand | 136 | 1 | 6 |
| β-strand | 137-139 | 3 | 7 |
| β-strand | 186 | 1 | 8 |
| β-strand | 187 | 1 | 9 |
| α-helix | 197-199 | 3 | |
| β-strand | 204-205 | 2 | 8 |
| β-strand | 212 | 1 | 10 |
| β-strand | 214-215 | 2 | 8 |
| α-helix | 221 | 1 | |
| β-strand | 222 | 1 | 10 |
| α-helix | 223 | 1 | |
| β-strand | 233 | 1 | 11 |
| β-strand | 234 | 1 | 6 |
| β-strand | 359 | 1 | 11 |
| β-strand | 436 | 1 | 5 |
| β-strand | 437 | 1 | 9 |
| β-strand | 448-450 | 3 | 7 |
| α-helix | 460-462 | 3 | |
| α-helix | 480-499 | 20 | |
Chain M: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 134-143 | 10 | |
| α-helix | 153-161 | 9 | |
Chain N: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 123-128 | 6 | |
| α-helix | 131-141 | 11 | |
| α-helix | 153-158 | 6 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Histone-lysine N-methyltransferase, H3 lysine-4 specific | E | protein | 278 | Saccharomyces cerevisiae (strain YJM789) | A6ZT27 (AlphaFold model) |
| COMPASS component BRE2 | K | protein | 417 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P43132 (AlphaFold model) |
| COMPASS component SDC1 | M, N | protein | 42 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q03323 (AlphaFold model) |
| COMPASS component SPP1 | F | protein | 237 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q03012 (AlphaFold model) |
| COMPASS component SWD1 | B | protein | 412 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P39706 |
| COMPASS component SWD3 | A | protein | 314 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P38123 |
Sequence of entity 1 (E), FASTA
>6BX3_1 Histone-lysine N-methyltransferase, H3 lysine-4 specific (chains E)
KIWQSRRKTLEEEKASDWQIELNGTLFDSELQPGSSFKAEGFRKVTDKLKINYLPHRRRV
HQPLNTVNIHNERNEYTPELCQREESSNKEPSDSVPQEVSSSRDNRASNRRFQQDIEAQK
AAIGTESELLSLNQLNKRKKPVMFARSAIHNWGLYALDSIAAKEMIIEYVGERIRQPVAE
MREKRYLKNGIGSSYLFRVDENTVIDATKKGGIARFINHCCDPNCTAKIIKVGGRRRIVI
YALRDIAASEELTYDYKFEREKDDEERLPCLCGAPNCK
Sequence of entity 2 (K), FASTA
>6BX3_2 COMPASS component BRE2 (chains K)
FDHSGMSVMDRSEGLSISRDGNDLVSVPDQYGWRTARSDVCIKEGMTYWEVEVIRGGNKK
FADGVNNKENADDSVDEVQSGIYEKMHKQVNDTPHLRFGVCRREASLEAPVGFDVYGYGI
RDISLESIHEGKLNCVLENGSPLKEGDKIGFLLSLPSIHTQIKQAKEFTKRRIFALNSHM
DTMNEPWREDAENGPSRKKLKQETTNKEFQRALLEDIEYNDVVRDQIAIRYKNQLFFEAT
DYVKTTKPEYYSSDKRERQDYYQLEDSYLAIFQNGKYLGKAFENLKPLLPPFSELQYNEK
FYLGYWQHGEARDESNDKNTTSAKKKKQQQKKKKGLILRNKYVNNNKLGYYPTISCFNGG
TARIISEEDKLEYLDQIRSAYCVDGNSKVNTLDTLYKEQIAEDIVWDIIDELEQIAL
Sequence of entity 3 (M, N), FASTA
>6BX3_3 COMPASS component SDC1 (chains M, N)
TRKYLNTNVTPHLLAGMRLIAVQQPEDPLRVLGEYLIEQSNI
Sequence of entity 4 (F), FASTA
>6BX3_4 COMPASS component SPP1 (chains F)
HGREFVNDIWSRLKTDEDRAVVKKMVEQTGHIDKFKKFGQLDFIDNNIVVKTDDEKEIFD
QIVVRDMTLKTLEDDLQEVQEISLPLFKKKLELLEVYLGWLDNVYTEMRKLDDDAASHVE
CGKEDSKGTKRKKKKNSSRSRARKNICGYCSTYERIPCSVEEFVRDFGSNEEATKIHEVC
TKWKCNRHLDWVSTNQEQYLQQIDSLESMQERLQHLIQARKKQLNIQYYEEILRRGL
Sequence of entity 5 (B), FASTA
>6BX3_5 COMPASS component SWD1 (chains B)
NILLQDPFAVLKEHPEKLTHTIENPLRTECLQFSPCGDYLALGCANGALVIYDMDTFRPI
CVPGNMLGAHVRPITSIAWSPDGRLLLTSSRDWSIKLWDLSKPSKPLKEIRFDSPIWGCQ
WLDAKRRLCVATIFEESDAYVIDFSNDPVASLLSKSDEKQLSSTPDHGYVLVCTVHTKHP
NIIIVGTSKGWLDFYKFHSLYQTECIHSLKITSSNIKHLIVSQNGERLAINCSDRTIRQY
EISIDDENSAVELTLEHKYQDVINKLQWNCILFSNNTAEYLVASTHGSSAHELYIWETTS
GTLVRVLEGAEEELIDINWDFYSMSIVSNGFESGNVYVWSVVIPPKWSALAPDFEEVEEN
VDYLEKEDEFDEVDEAEQQQGLEQEEEIAIDLRTREQYDVRGNNLLVERFTI
Sequence of entity 6 (A), FASTA
>6BX3_6 COMPASS component SWD3 (chains A)
FQFVTPVGTQNGLKATCAKISPDGQFLAITQGLNILIYDINRRTVSQTLVTSHARPFSEL
CWSPDGQCIATASDDFSVEIIHLSYGLLHTFIGHTAPVISLTFNRKGNLLFTSSMDESIK
IWDTLNGSLMKTISAHSEAVVSVDVPMNDSSILSSGSYDGLIRIFDAETGHCLKTLTYDK
DWKRENGVVPISQVKFSENARYLLVKSLDGVVKIWDCIGGCVVRTFQVQPLEKGVLHHSC
GMDFLNPEDGSTPLVISGYENGDIYCWNSDTKSLLQLLDGSLYHHSSPVMSIHCFGNIMC
SLALNGDCCLWRWV
Primary citation
Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex. Qu, Q., Takahashi, Y.H., Yang, Y. et al. Cell (2018) 174:1117-1126.e12. DOI 10.1016/j.cell.2018.07.020 · PubMed
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