Research workbench
Computational design and crystal structure of an enhanced affinity mutant human CD8-alpha-alpha co-receptor
Analyse Computational design and crystal structure of an enhanced affinity mutant human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HP4
- Type
- protein
- Length
- 228 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01732
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 114 | — | P01732 |
Compared structures
- 2HP4 · Computational design and crystal structure of an enhanced affinity mutant human… · the same entry in another collection · chain A against A, TM-score 1.00
- P01732 · AlphaFold monomer V2.0 prediction for T-cell surface glycoprotein CD8 alpha chain (P01732) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P01732
- Elsewhere: RCSB PDB 2HP4 · PDBe 2HP4 · UniProt P01732
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