Research workbench
Crystal structure determination of HLA-A2.1 complexed to GP2 peptide VARIANT(I2L/V5L)
Analyse Crystal structure determination of HLA-A2.1 complexed to GP2 peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EEZ
- Type
- protein
- Length
- 768 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01892, P01884
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 275 | — | P01892 |
| B, E | — | protein | 100 | — | P01884 |
| C, F | — | protein | 9 | — | — |
Compared structures
- 1EEZ · Crystal Structure Determination of HLA-A2.1 Complexed to GP2 Peptide Variant(I2L/V5L) · the same entry in another collection · chain A against A, 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 P01892
- Every structure of UniProt P01884
- Elsewhere: RCSB PDB 1EEZ · PDBe 1EEZ · UniProt P01892 · UniProt P01884
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