MolNFT v2 · #159108 · protein
Atomic structures and deletion mutant reveal different capsid-binding patterns and functional significance of tegument protein pp150 in murine and human cytomegaloviruses with implications for therapeutic development
6NHJ: “Atomic structures and deletion mutant reveal different capsid-binding patterns and functional significance of…”. Electron microscopy at 5.0. MolNFT v2 #159108 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6NHJ
- Type
- protein
- Length
- 27,627 residues
- Chains
- 55
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 5.0
- Source
- Murine cytomegalovirus (strain Smith)
- UniProt
- A0A1S5YGR4, D3XDM2, D3XDN6, D3XDN4, D3XDR2
Structure
electron microscopy · resolution 5.0 · 31 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1335 | — | A0A1S5YGR4 |
| B | — | protein | 1310 | — | A0A1S5YGR4 |
| C | — | protein | 1310 | — | A0A1S5YGR4 |
| D | — | protein | 1314 | — | A0A1S5YGR4 |
| E | — | protein | 1330 | — | A0A1S5YGR4 |
| F | — | protein | 1319 | — | A0A1S5YGR4 |
| G, H | — | protein | 1341 | — | A0A1S5YGR4 |
| I | — | protein | 1321 | — | A0A1S5YGR4 |
| k | — | protein | 1295 | — | A0A1S5YGR4 |
| l | — | protein | 1336 | — | A0A1S5YGR4 |
| m | — | protein | 1312 | — | A0A1S5YGR4 |
| n | — | protein | 1335 | — | A0A1S5YGR4 |
| o | — | protein | 1313 | — | A0A1S5YGR4 |
| p | — | protein | 1301 | — | A0A1S5YGR4 |
| q | — | protein | 1219 | — | A0A1S5YGR4 |
| 2, e, f, g | — | protein | 174 | — | D3XDM2 |
| 3, h, i, j | — | protein | 200 | — | D3XDM2 |
| J, r, u, v, w | — | protein | 60 | — | D3XDN6 |
| K, L, M, N, O, P, Q, R, s, t | — | protein | 59 | — | D3XDN6 |
| x | — | protein | 57 | — | D3XDN6 |
| y | — | protein | 249 | — | D3XDN4 |
| S, T, U, V | — | protein | 289 | — | D3XDN4 |
| z | — | protein | 284 | — | D3XDR2 |
| W, Z | — | protein | 281 | — | D3XDR2 |
| X | — | protein | 277 | — | D3XDR2 |
| Y | — | protein | 282 | — | D3XDR2 |
| 1 | — | protein | 257 | — | D3XDR2 |
| a | — | protein | 267 | — | D3XDR2 |
| b | — | protein | 270 | — | D3XDR2 |
| c | — | protein | 274 | — | D3XDR2 |
| d | — | protein | 274 | — | D3XDR2 |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A1S5YGR4
- Every structure of UniProt D3XDM2
- Every structure of UniProt D3XDN6
- Every structure of UniProt D3XDN4
- Every structure of UniProt D3XDR2
- Elsewhere: RCSB PDB 6NHJ · PDBe 6NHJ · UniProt A0A1S5YGR4 · UniProt D3XDM2 · UniProt D3XDN6 · UniProt D3XDN4 · UniProt D3XDR2
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