Research workbench
X-ray crystallographic structural characteristics of arabidopsis hemoglobin I and their functional implications
Analyse X-ray crystallographic structural characteristics of arabidopsis hemoglobin I… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZHW
- Type
- protein
- Length
- 307 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O24520
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 154 | — | O24520 |
| B | — | protein | 153 | — | O24520 |
Compared structures
- 3ZHW · X-ray Crystallographic Structural Characteristics of Arabidopsis Hemoglobin I and their… · the same entry in another collection · chain A against A, TM-score 1.00
- O24520 · AlphaFold monomer V2.0 prediction for non-symbiotic hemoglobin 1 (O24520) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 O24520
- Elsewhere: RCSB PDB 3ZHW · PDBe 3ZHW · UniProt O24520
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