Research workbench
Crystal structure of the epstein-barr virus gh and gl complex
Analyse Crystal structure of the epstein-barr virus gh and gl complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PHF
- Type
- protein
- Length
- 12,176 residues
- Chains
- 32
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P03231, P03212
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K, M, O, Q, S, U, W, Y, 1, 3, 5 | — | protein | 653 | — | P03231 |
| B, D, F, H, J, L, N, P, R, T, V, X, Z, 2, 4, 6 | — | protein | 108 | — | P03212 |
Compared structures
- 3PHF · Crystal Structure of the Epstein-Barr virus gH and gL complex · the same entry in another collection · chain B against B, TM-score 1.00
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 P03231
- Every structure of UniProt P03212
- Elsewhere: RCSB PDB 3PHF · PDBe 3PHF · UniProt P03231 · UniProt P03212
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