Research workbench
High-resolution X-ray study of deoxy recombinant human hemoglobins synthesized from beta-globins having mutated amino termini
Analyse High-resolution X-ray study of deoxy recombinant human hemoglobins synthesized… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DXU
- Type
- protein
- Length
- 574 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P69905, P68871
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 141 | — | P69905 |
| B, D | — | protein | 146 | — | P68871 |
Compared structures
- 1DXU · High-resolution X-ray study of deoxy recombinant human hemoglobins synthesized from… · the same entry in another collection · chain C against C, 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 P69905
- Every structure of UniProt P68871
- Elsewhere: RCSB PDB 1DXU · PDBe 1DXU · UniProt P69905 · UniProt P68871
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