Crystal structure of NRMT1 in complex with SPKRIA peptide. Determined by X-ray diffraction at 1.65 Å resolution. Released 28 Oct 2015.
Explore 5E1B in 3D Show helices and sheets RCSB PDB PDBe
5E1B contains 33 α-helices and 22 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 |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| α-helix | 9-21 | 13 | |
| α-helix | 27-30 | 4 | |
| α-helix | 35-37 | 3 | |
| α-helix | 38-50 | 13 | |
| α-helix | 51-53 | 3 | |
| β-strand | 64-68 | 5 | 1 |
| α-helix | 74-75 | 2 | |
| α-helix | 76-80 | 5 | |
| β-strand | 86-91 | 6 | 1 |
| α-helix | 94-103 | 10 | |
| α-helix | 105-110 | 6 | |
| β-strand | 111-116 | 6 | 1 |
| α-helix | 119-121 | 3 | |
| α-helix | 124-125 | 2 | |
| β-strand | 129-135 | 7 | 1 |
| α-helix | 138-140 | 3 | |
| α-helix | 143-156 | 14 | |
| β-strand | 157-170 | 14 | 1 |
| β-strand | 174-177 | 4 | 1 |
| β-strand | 182-186 | 5 | 1 |
| α-helix | 187-196 | 10 | |
| β-strand | 201-206 | 6 | 1 |
| α-helix | 207-208 | 2 | |
| β-strand | 214 | 1 | 2 |
| α-helix | 215 | 1 | |
| β-strand | 216-222 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-5 | 4 | |
| α-helix | 9-21 | 13 | |
| α-helix | 27-30 | 4 | |
| α-helix | 35-37 | 3 | |
| α-helix | 38-54 | 17 | |
| β-strand | 64-68 | 5 | 3 |
| α-helix | 74-75 | 2 | |
| α-helix | 76-80 | 5 | |
| β-strand | 86-91 | 6 | 3 |
| α-helix | 94-103 | 10 | |
| α-helix | 105-110 | 6 | |
| β-strand | 111-116 | 6 | 3 |
| α-helix | 119-121 | 3 | |
| α-helix | 124-125 | 2 | |
| β-strand | 129-135 | 7 | 3 |
| α-helix | 138-140 | 3 | |
| α-helix | 143-156 | 14 | |
| β-strand | 157-169 | 13 | 3 |
| β-strand | 174-177 | 4 | 3 |
| β-strand | 182-185 | 4 | 3 |
| α-helix | 187-196 | 10 | |
| β-strand | 201-206 | 6 | 3 |
| α-helix | 207-208 | 2 | |
| β-strand | 214 | 1 | 4 |
| α-helix | 215 | 1 | |
| β-strand | 216-222 | 7 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| N-terminal Xaa-Pro-Lys N-methyltransferase 1 | A, B | protein | 241 | Homo sapiens | Q9BV86 (AlphaFold model) |
| RCC1 | D, E | protein | 6 | Homo sapiens | P18754 (AlphaFold model) |
>5E1B_1 N-terminal Xaa-Pro-Lys N-methyltransferase 1 (chains A, B) MGSSHHHHHHSSGLVPRGSTSEVIEDEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDI NSSRKFLQRFLREGPNKTGTSCALDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKT YLGEEGKRVRNYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGI IVIKDNMAQEGVILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIYHVYSFAL R
>5E1B_2 RCC1 (chains D, E) SPKRIA
| ID | Name | Formula | Copies |
|---|---|---|---|
| SAH | S-adenosyl-L-homocysteine | C14 H20 N6 O5 S | 2 |
Water and common crystallization additives (UNX, GOL) are not listed.
Structural basis for substrate recognition by the human N-terminal methyltransferase 1. Dong, C., Mao, Y., Tempel, W. et al. Genes Dev (2015) 29:2343-2348. DOI 10.1101/gad.270611.115 · PubMed
Other PDB entries of the same protein (UniProt Q9BV86 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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