Research workbench
HLA-DR1 with covalently linked CLIP106-120 in reversed orientation
Analyse HLA-DR1 with covalently linked CLIP106-120 in reversed orientation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AEN
- Type
- protein
- Length
- 374 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01903, P04229, P04233
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 178 | — | P01903 |
| B | — | protein | 181 | — | P04229 |
| C | — | protein | 15 | — | P04233 |
Compared structures
- 4AEN · HLA-DR1 with covalently linked CLIP106-120 in reversed orientation · the same entry in another collection · chain A against A, TM-score 1.00
- P01903 · AlphaFold monomer V2.0 prediction for HLA class II histocompatibility antigen, dr alpha… · a predicted model of the same protein · chain A against A, TM-score 0.97
- P04233 · AlphaFold monomer V2.0 prediction for HLA class II histocompatibility antigen gamma chain… · a predicted model of the same protein · chain C against A, TM-score 0.27
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 P01903
- Every structure of UniProt P04229
- Every structure of UniProt P04233
- Elsewhere: RCSB PDB 4AEN · PDBe 4AEN · UniProt P01903 · UniProt P04229 · UniProt P04233
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