Crystal Structure of POMGNT2 in complex with UDP and mono-mannosyl peptide (379Man short peptide). Determined by X-ray diffraction at 2.1 Å resolution. Released 5 May 2021.
Explore 7E9L in 3D Show helices and sheets RCSB PDB PDBe
7E9L contains 62 α-helices and 66 β-strands across 3 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 | 53-63 | 11 | |
| β-strand | 64 | 1 | 1 |
| β-strand | 66-69 | 4 | 2 |
| α-helix | 74-76 | 3 | |
| β-strand | 79-82 | 4 | 2 |
| β-strand | 84-87 | 4 | 1 |
| β-strand | 92-97 | 6 | 1 |
| β-strand | 102-104 | 3 | 2 |
| α-helix | 108-112 | 5 | |
| β-strand | 117-118 | 2 | 3 |
| β-strand | 129-130 | 2 | 3 |
| β-strand | 132-136 | 5 | 1 |
| α-helix | 137-142 | 6 | |
| α-helix | 144-146 | 3 | |
| β-strand | 147-149 | 3 | 1 |
| β-strand | 153-156 | 4 | 2 |
| α-helix | 164-166 | 3 | |
| α-helix | 167-172 | 6 | |
| α-helix | 173-181 | 9 | |
| α-helix | 185-188 | 4 | |
| α-helix | 189 | 1 | |
| β-strand | 190-193 | 4 | 2 |
| α-helix | 203-208 | 6 | |
| α-helix | 213-214 | 2 | |
| β-strand | 215-216 | 2 | 2 |
| α-helix | 217-219 | 3 | |
| α-helix | 220-223 | 4 | |
| β-strand | 226-229 | 4 | 1 |
| β-strand | 232-234 | 3 | 2 |
| β-strand | 243-244 | 2 | 4 |
| β-strand | 252-253 | 2 | 4 |
| α-helix | 261-274 | 14 | |
| β-strand | 288-292 | 5 | 5 |
| β-strand | 300 | 1 | 6 |
| α-helix | 303-314 | 12 | |
| β-strand | 317-321 | 5 | 5 |
| α-helix | 328-336 | 9 | |
| β-strand | 340-344 | 5 | 5 |
| α-helix | 347-354 | 8 | |
| α-helix | 356 | 1 | |
| β-strand | 360-365 | 6 | 5 |
| α-helix | 371-373 | 3 | |
| α-helix | 376-382 | 7 | |
| β-strand | 389-394 | 6 | 5 |
| α-helix | 398-400 | 3 | |
| β-strand | 401-402 | 2 | 6 |
| α-helix | 409-411 | 3 | |
| α-helix | 419-427 | 9 | |
| α-helix | 431-433 | 3 | |
| α-helix | 440-446 | 7 | |
| β-strand | 449-450 | 2 | 6 |
| α-helix | 454-462 | 9 | |
| α-helix | 477-479 | 3 | |
| β-strand | 486-496 | 11 | 7 |
| β-strand | 499-507 | 9 | 7 |
| α-helix | 508-509 | 2 | |
| α-helix | 510-514 | 5 | |
| β-strand | 520-528 | 9 | 8 |
| β-strand | 534-539 | 6 | 8 |
| β-strand | 543-546 | 4 | 7 |
| β-strand | 555-564 | 10 | 8 |
| β-strand | 568-572 | 5 | 8 |
| α-helix | 573 | 1 | |
| α-helix | 575 | 1 | |
| β-strand | 576-579 | 4 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 53-58 | 6 | |
| α-helix | 59-63 | 5 | |
| β-strand | 64 | 1 | 9 |
| β-strand | 66-70 | 5 | 10 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-82 | 5 | 10 |
| β-strand | 84-87 | 4 | 9 |
| β-strand | 92-97 | 6 | 9 |
| β-strand | 102-104 | 3 | 10 |
| α-helix | 108-112 | 5 | |
| β-strand | 117-118 | 2 | 11 |
| β-strand | 129-130 | 2 | 11 |
| β-strand | 132-136 | 5 | 9 |
| α-helix | 137-142 | 6 | |
| α-helix | 144-146 | 3 | |
| β-strand | 147-149 | 3 | 9 |
| β-strand | 153-156 | 4 | 10 |
| α-helix | 164-166 | 3 | |
| α-helix | 167-172 | 6 | |
| α-helix | 173-179 | 7 | |
| α-helix | 185-188 | 4 | |
| β-strand | 190-193 | 4 | 10 |
| α-helix | 203-208 | 6 | |
| α-helix | 213-214 | 2 | |
| β-strand | 215-216 | 2 | 10 |
| α-helix | 217-223 | 7 | |
| β-strand | 226-229 | 4 | 9 |
| β-strand | 232-234 | 3 | 10 |
| β-strand | 243-244 | 2 | 12 |
| β-strand | 252-253 | 2 | 12 |
| α-helix | 261-274 | 14 | |
| β-strand | 288-292 | 5 | 13 |
| β-strand | 300 | 1 | 14 |
| α-helix | 303-314 | 12 | |
| β-strand | 317-321 | 5 | 13 |
| α-helix | 328-336 | 9 | |
| β-strand | 340-344 | 5 | 13 |
| α-helix | 347-354 | 8 | |
| α-helix | 356 | 1 | |
| β-strand | 360-365 | 6 | 13 |
| α-helix | 371-373 | 3 | |
| α-helix | 376-381 | 6 | |
| β-strand | 389-394 | 6 | 13 |
| β-strand | 401-402 | 2 | 14 |
| α-helix | 409-411 | 3 | |
| α-helix | 419-427 | 9 | |
| α-helix | 431-433 | 3 | |
| α-helix | 440-446 | 7 | |
| β-strand | 449-450 | 2 | 14 |
| α-helix | 454-462 | 9 | |
| α-helix | 480-482 | 3 | |
| β-strand | 486-492 | 7 | 15 |
| β-strand | 502-507 | 6 | 15 |
| α-helix | 508-509 | 2 | |
| α-helix | 510-514 | 5 | |
| β-strand | 520-528 | 9 | 16 |
| β-strand | 535-539 | 5 | 16 |
| β-strand | 543-546 | 4 | 15 |
| β-strand | 555-564 | 10 | 16 |
| β-strand | 568-572 | 5 | 16 |
| α-helix | 575 | 1 | |
| β-strand | 576-579 | 4 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-10 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 | A, B | protein | 539 | Bos taurus | Q5NDF2 (AlphaFold model) |
| mono-mannosyl peptide (379Man short peptide) | C | protein | 14 | Homo sapiens | Q14118 (AlphaFold model) |
>7E9L_1 Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 (chains A, B) GAPPAPALRIDYPKALQILTEGGTHMVCTGRTHTDRLCRFKWLCYSSEAEEFIFFHGNAS VMLPSLGSRRFQPALLDLSTVEDHNTQYFNFVELPAAALRFMPKPVFVPDVALIANRFNP DNLMHVFHDDLLPLFYTLRQFPGLAREARLFFMEGWGEGAHFDLYKLLSPKQPLLRAQLK ALGRLLCFSHAFVGLSKVTTWYQYGFVQPQGPKANILVSGNEIRQFAHFLMEKLNVSQAG GPLGEEYILVFSRTQNRLILNEAELLLALAQEFQMKTVTVSLEDHAFADVVRLVSNASML VSMHGAQLVTALFLPRGAAVVELFPYAVNPDHYTPYKTLATLPGMDLQYIAWQNTMPENT VTHPERPWDQGGIAHLDRAEQARILQSREVPRHLCCRNPEWLFRIYQDTKVDIPSLIQTI RRVVKGHPGPRKQKWTVSLYPGKVREARCQASVQGASEARLSVSWQIPWNLKYLKVREVK YEVWLQEQGENTYVPYMLALQNHTFTENIKPFTTYLVWIRCIFNKTLLGPFADVLVCST
>7E9L_2 mono-mannosyl peptide (379Man short peptide) (chains C) XQTPTLGPIQPTRX
| ID | Name | Formula | Copies |
|---|---|---|---|
| MAN | alpha-D-mannopyranose | C6 H12 O6 | 1 |
| UDP | Uridine-5'-diphosphate | C9 H14 N2 O12 P2 | 2 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 5 |
Water and common crystallization additives (TRS) are not listed.
The structure of POMGNT2 provides new insights into the mechanism to determine the functional O-mannosylation site on alpha-dystroglycan. Imae, R., Kuwabara, N., Manya, H. et al. Genes Cells (2021) 26:485-494. DOI 10.1111/gtc.12853 · PubMed
Other PDB entries of the same protein (UniProt Q5NDF2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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