Crystal structure of human NDRG3 C30S mutant. Determined by X-ray diffraction at 3.4 Å resolution. Released 26 Aug 2020.
Explore 6L4H in 3D Show helices and sheets RCSB PDB PDBe
6L4H contains 78 α-helices and 38 β-strands across 4 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 |
|---|---|---|---|
| β-strand | 32-37 | 6 | 1 |
| β-strand | 40-47 | 8 | 1 |
| α-helix | 54-55 | 2 | |
| β-strand | 56-60 | 5 | 1 |
| α-helix | 61-62 | 2 | |
| α-helix | 67-75 | 9 | |
| α-helix | 78-86 | 9 | |
| β-strand | 89-93 | 5 | 1 |
| α-helix | 101-105 | 5 | |
| α-helix | 110-112 | 3 | |
| α-helix | 113-117 | 5 | |
| α-helix | 120-126 | 7 | |
| β-strand | 132-137 | 6 | 1 |
| α-helix | 139-150 | 12 | |
| β-strand | 155-161 | 7 | 1 |
| α-helix | 167-169 | 3 | |
| α-helix | 185-193 | 9 | |
| α-helix | 196-201 | 6 | |
| α-helix | 204-215 | 12 | |
| α-helix | 219-230 | 12 | |
| α-helix | 239-241 | 3 | |
| β-strand | 255-261 | 7 | 1 |
| α-helix | 267-274 | 8 | |
| α-helix | 279-281 | 3 | |
| β-strand | 282-287 | 6 | 1 |
| α-helix | 294-297 | 4 | |
| α-helix | 299-313 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 30-37 | 8 | 2 |
| β-strand | 40-47 | 8 | 2 |
| α-helix | 49-51 | 3 | |
| α-helix | 55 | 1 | |
| β-strand | 56-60 | 5 | 2 |
| α-helix | 67 | 1 | |
| α-helix | 68-72 | 5 | |
| α-helix | 73-76 | 4 | |
| α-helix | 78-84 | 7 | |
| β-strand | 89-93 | 5 | 2 |
| α-helix | 101-105 | 5 | |
| α-helix | 110-112 | 3 | |
| α-helix | 113-118 | 6 | |
| α-helix | 120-126 | 7 | |
| β-strand | 132-137 | 6 | 2 |
| α-helix | 139-150 | 12 | |
| β-strand | 155-161 | 7 | 2 |
| α-helix | 185-193 | 9 | |
| α-helix | 196-201 | 6 | |
| α-helix | 204-215 | 12 | |
| α-helix | 219-230 | 12 | |
| α-helix | 232-234 | 3 | |
| β-strand | 237 | 1 | 3 |
| α-helix | 239-241 | 3 | |
| β-strand | 250 | 1 | 3 |
| β-strand | 255-261 | 7 | 2 |
| α-helix | 267-275 | 9 | |
| α-helix | 279-281 | 3 | |
| β-strand | 282-287 | 6 | 2 |
| α-helix | 294-297 | 4 | |
| α-helix | 299-313 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 32-37 | 6 | 4 |
| β-strand | 40-47 | 8 | 4 |
| α-helix | 55 | 1 | |
| β-strand | 56-60 | 5 | 4 |
| α-helix | 67 | 1 | |
| α-helix | 68-72 | 5 | |
| α-helix | 73-76 | 4 | |
| α-helix | 78-86 | 9 | |
| β-strand | 89-93 | 5 | 4 |
| α-helix | 101-105 | 5 | |
| α-helix | 110-112 | 3 | |
| α-helix | 113-117 | 5 | |
| α-helix | 120-126 | 7 | |
| β-strand | 132-137 | 6 | 4 |
| α-helix | 139-150 | 12 | |
| β-strand | 155-161 | 7 | 4 |
| α-helix | 167-168 | 2 | |
| α-helix | 185-193 | 9 | |
| α-helix | 196-201 | 6 | |
| α-helix | 204-215 | 12 | |
| α-helix | 219-230 | 12 | |
| α-helix | 232-234 | 3 | |
| β-strand | 237 | 1 | 5 |
| β-strand | 250 | 1 | 5 |
| β-strand | 255-261 | 7 | 4 |
| α-helix | 267-275 | 9 | |
| β-strand | 282-287 | 6 | 4 |
| α-helix | 294-297 | 4 | |
| α-helix | 299-313 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 30-35 | 6 | 6 |
| β-strand | 42-47 | 6 | 6 |
| α-helix | 55 | 1 | |
| β-strand | 56-60 | 5 | 6 |
| α-helix | 67 | 1 | |
| α-helix | 68-72 | 5 | |
| α-helix | 73-76 | 4 | |
| α-helix | 78-86 | 9 | |
| β-strand | 89-93 | 5 | 6 |
| α-helix | 101-105 | 5 | |
| α-helix | 110-112 | 3 | |
| α-helix | 113-118 | 6 | |
| α-helix | 120-126 | 7 | |
| β-strand | 132-137 | 6 | 6 |
| α-helix | 139-150 | 12 | |
| α-helix | 152-154 | 3 | |
| β-strand | 155-161 | 7 | 6 |
| α-helix | 185-193 | 9 | |
| α-helix | 196-201 | 6 | |
| α-helix | 204-216 | 13 | |
| α-helix | 219-231 | 13 | |
| β-strand | 237 | 1 | 7 |
| α-helix | 239-241 | 3 | |
| β-strand | 250 | 1 | 7 |
| β-strand | 255-261 | 7 | 6 |
| α-helix | 267-276 | 10 | |
| β-strand | 282-287 | 6 | 6 |
| α-helix | 294-297 | 4 | |
| α-helix | 299-311 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein NDRG3 | A, B, C, D | protein | 375 | Homo sapiens | Q9UGV2 (AlphaFold model) |
>6L4H_1 Protein NDRG3 (chains A, B, C, D) MDELQDVQLTEIKPLLNDKNGTRNFQDFDSQEHDIETTHGVVHVTIRGLPKGNRPVILTY HDIGLNHKSCFNAFFNFEDMQEITQHFAVCHVDAPGQQEGAPSFPTGYQYPTMDELAEML PPVLTHLSLKSIIGIGVGAGAYILSRFALNHPELVEGLVLINVDPCAKGWIDWAASKLSG LTTNVVDIILAHHFGQEELQANLDLIQTYRMHIAQDINQDNLQLFLNSYNGRRDLEIERP ILGQNDNKSKTLKCSTLLVVGDNSPAVEAVVECNSRLNPINTTLLKMADCGGLPQVVQPG KLTEAFKYFLQGMGYIPSASMTRLARSRTHSTSSSLGSGESPFSRSVTSNQSDGTQESCE SPDVLDRHQTMEVSC
Structural and Biophysical Analyses of Human N-Myc Downstream-Regulated Gene 3 (NDRG3) Protein. Kim, K.R., Kim, K.A., Park, J.S. et al. Biomolecules (2020) 10. DOI 10.3390/biom10010090 · PubMed
Other PDB entries of the same protein (UniProt Q9UGV2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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