Research workbench
The three-dimensional structure of an H-2LD peptide complex explains the unique interaction of ld with BETA2M and peptide
Analyse The three-dimensional structure of an H-2LD peptide complex explains the unique… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LD9
- Type
- protein
- Length
- 752 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01897, P01887
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 268 | — | P01897 |
| B, E | — | protein | 99 | — | P01887 |
| C, F | — | protein | 9 | — | — |
Compared structures
- 1LD9 · The three-dimensional structure of an H-2LD peptide complex explains the unique… · the same entry in another collection · chain F against F, TM-score 1.00
- P01887 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P01887) · a predicted model of the same protein · chain B against A, TM-score 0.98
- P01897 · AlphaFold monomer V2.0 prediction for H-2 class I histocompatibility antigen, L-D alpha… · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P01897
- Every structure of UniProt P01887
- Elsewhere: RCSB PDB 1LD9 · PDBe 1LD9 · UniProt P01897 · UniProt P01887
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