Research workbench
Trout hemoglobin I
Analyse Trout hemoglobin I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OUT
- Type
- protein
- Length
- 288 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin I
- UniProt
- P02019, P02142
- Ligands
- HEM, ACE
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemoglobin I | protein | 142 | 77% helix, 0% strand | P02019 |
| B | Hemoglobin I | protein | 146 | 78% helix, 0% strand | P02142 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- ACE · Acetyl group · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 199 | 0.75 | 0.90 | 26 | HEM |
| 2 | 68 | 0.68 | 0.94 | 16 | empty |
| 3 | 197 | 0.67 | 0.85 | 26 | HEM |
| 4 | 180 | 0.49 | 0.77 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 889 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1OUT · Trout hemoglobin I · the same entry in another collection · chain A against A, TM-score 1.00
- P02142 · AlphaFold monomer V2.0 prediction for hemoglobin subunit beta-1 (P02142) · a predicted model of the same protein · chain B against A, TM-score 0.99
- P02019 · AlphaFold monomer V2.0 prediction for hemoglobin subunit alpha-1 (P02019) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P02019
- Every structure of UniProt P02142
- Elsewhere: RCSB PDB 1OUT · PDBe 1OUT · UniProt P02019 · UniProt P02142
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