Research workbench
The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: oxygenated form
Analyse The structure of a deoxygenated 400 kda hemoglobin provides a more accurate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WCT
- Type
- protein
- Length
- 1,174 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- S0BBU7, S0BBR6, S0BCU7, S0BAP9
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | — | protein | 146 | — | S0BBU7 |
| B, F | — | protein | 144 | — | S0BBR6 |
| C, G | — | protein | 150 | — | S0BCU7 |
| D, H | — | protein | 147 | — | S0BAP9 |
Compared structures
- 3WCT · The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description… · the same entry in another collection · chain F against F, 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 S0BBU7
- Every structure of UniProt S0BBR6
- Every structure of UniProt S0BCU7
- Every structure of UniProt S0BAP9
- Elsewhere: RCSB PDB 3WCT · PDBe 3WCT · UniProt S0BBU7 · UniProt S0BBR6 · UniProt S0BCU7 · UniProt S0BAP9
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