Crystal structure of the human MTERF4:NSUN4:SAM ternary complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 3 Oct 2012.
Explore 4FZV in 3D Show helices and sheets RCSB PDB PDBe
4FZV contains 43 α-helices and 17 β-strands across 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 40-56 | 17 | |
| α-helix | 57-59 | 3 | |
| α-helix | 60-67 | 8 | |
| α-helix | 70-72 | 3 | |
| β-strand | 74-77 | 4 | 1 |
| α-helix | 83-92 | 10 | |
| β-strand | 96-97 | 2 | 1 |
| α-helix | 98-104 | 7 | |
| α-helix | 121-124 | 4 | |
| β-strand | 131-133 | 3 | 1 |
| α-helix | 134-135 | 2 | |
| α-helix | 142-145 | 4 | |
| β-strand | 147 | 1 | 2 |
| β-strand | 153 | 1 | 2 |
| β-strand | 155-158 | 4 | 1 |
| α-helix | 160-162 | 3 | |
| α-helix | 163-169 | 7 | |
| β-strand | 175-179 | 5 | 3 |
| α-helix | 186-193 | 8 | |
| β-strand | 197-203 | 7 | 3 |
| α-helix | 207-220 | 14 | |
| β-strand | 231-234 | 4 | 3 |
| α-helix | 238-240 | 3 | |
| α-helix | 241-244 | 4 | |
| β-strand | 249-255 | 7 | 3 |
| α-helix | 261-264 | 4 | |
| α-helix | 275-277 | 3 | |
| α-helix | 278-282 | 5 | |
| α-helix | 284-297 | 14 | |
| β-strand | 299-309 | 11 | 3 |
| α-helix | 318-332 | 15 | |
| β-strand | 336-338 | 3 | 3 |
| α-helix | 342-348 | 7 | |
| β-strand | 353-354 | 2 | 3 |
| β-strand | 362-365 | 4 | 3 |
| β-strand | 367 | 1 | 4 |
| β-strand | 370 | 1 | 4 |
| β-strand | 375-382 | 8 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 95-104 | 10 | |
| α-helix | 111-118 | 8 | |
| α-helix | 126-134 | 9 | |
| α-helix | 140-146 | 7 | |
| α-helix | 149-152 | 4 | |
| α-helix | 156-166 | 11 | |
| α-helix | 167-171 | 5 | |
| α-helix | 177-182 | 6 | |
| α-helix | 184-187 | 4 | |
| α-helix | 191-204 | 14 | |
| α-helix | 209-218 | 10 | |
| α-helix | 220-223 | 4 | |
| α-helix | 226 | 1 | |
| α-helix | 229-235 | 7 | |
| α-helix | 236-240 | 5 | |
| α-helix | 245-250 | 6 | |
| α-helix | 253-255 | 3 | |
| α-helix | 258-271 | 14 | |
| α-helix | 290-294 | 5 | |
| α-helix | 298-300 | 3 | |
| α-helix | 301-305 | 5 | |
| α-helix | 310-327 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Putative methyltransferase NSUN4 | A | protein | 359 | Homo sapiens | Q96CB9 (AlphaFold model) |
| mTERF domain-containing protein 2 | B | protein | 239 | Homo sapiens | Q7Z6M4 (AlphaFold model) |
>4FZV_1 Putative methyltransferase NSUN4 (chains A) RYKKKWAATEPKFPAVRLALQNFDMTYSVQFGDLWPSIRVSLLSEQKYGALVNNFAAWDH VSAKLEQLSAKDFVNEAISHWELQSEGGQSAAPSPASWACSPNLRCFTFDRGDISRFPPA RPGSLGVMEYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQTGCCRNLAANDL SPSRIARLQKILHSYVPEEIRDGNQVRVTSWDGRKWGELEGDTYDRVLVDVPCTTDRHSL HEEENNIFKRSRKKERQILPVLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQGAI ELLANQYSIQVQVEDLTHFRRVFMDTFCFFSSCQVGELVIPNLMANFGPMYFCKMRRLT
>4FZV_2 mTERF domain-containing protein 2 (chains B) XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQQLLDIISEFILLGLNPEPVCVVLKKSPQL LKLPIMQMRKRSSYLQKLGLGEGKLKRVLYCCPEIFTMRQQDINDTVRLLKEKCLFTVQQ VTKILHSCPSVLREDLGQLEYKFQYAYFRMGIKHPDIVKSEYLQYSLTKIKQRHIYLERL GRYQTPDKKGQTQIPNPLLKDILRVSEAEFLARTACTSVEEFQVFKKLLAREEEESESS
| ID | Name | Formula | Copies |
|---|---|---|---|
| SAM | S-adenosylmethionine | C15 H22 N6 O5 S | 1 |
Water and common crystallization additives (FMT, EDO) are not listed.
Structure of the Essential MTERF4:NSUN4 Protein Complex Reveals How an MTERF Protein Collaborates to Facilitate rRNA Modification. Yakubovskaya, E., Guja, K.E., Mejia, E. et al. Structure (2012) 20:1940-1947. DOI 10.1016/j.str.2012.08.027 · PubMed
Other PDB entries of the same protein (UniProt Q96CB9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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