Research workbench
Cryo-EM structure of the hcmv ghglgo trimer derived from AD169 and tr strains in complex with pdgfralpha
Analyse Cryo-EM structure of the hcmv ghglgo trimer derived from AD169 and tr strains… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RAM
- Type
- protein
- Length
- 1,497 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P12824, P16832, Q8AZ32, P16234
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 674 | — | P12824 |
| B | — | protein | 237 | — | P16832 |
| C | — | protein | 297 | — | Q8AZ32 |
| D | — | protein | 289 | — | P16234 |
Compared structures
- 7RAM · Cryo-EM Structure of the HCMV gHgLgO Trimer Derived from AD169 and TR strains in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- P16234 · AlphaFold monomer V2.0 prediction for platelet-derived growth factor receptor alpha… · a predicted model of the same protein · chain D against A, TM-score 0.62
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 P12824
- Every structure of UniProt P16832
- Every structure of UniProt Q8AZ32
- Every structure of UniProt P16234
- Elsewhere: RCSB PDB 7RAM · PDBe 7RAM · UniProt P12824 · UniProt P16832 · UniProt Q8AZ32 · UniProt P16234
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