Research workbench
Site-selective glycosylation of cysteine-93 beta on the surface of bovine hemoglobin and its application as a novel oxygen therapeutic
Analyse Site-selective glycosylation of cysteine-93 beta on the surface of bovine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CIU
- Type
- protein
- Length
- 571 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01966, P02070
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 140 | — | P01966 |
| B, D | — | protein | 145 | — | P02070 |
| C | — | protein | 141 | — | P01966 |
Compared structures
- 3CIU · Site-Selective Glycosylation of Cysteine-93 beta on the Surface of Bovine Hemoglobin and… · the same entry in another collection · chain A against A, TM-score 1.00
- P02070 · AlphaFold monomer V2.0 prediction for hemoglobin subunit beta (P02070) · a predicted model of the same protein · chain B against A, TM-score 0.98
- P01966 · AlphaFold monomer V2.0 prediction for hemoglobin subunit alpha (P01966) · 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 P01966
- Every structure of UniProt P02070
- Elsewhere: RCSB PDB 3CIU · PDBe 3CIU · UniProt P01966 · UniProt P02070
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