Research workbench
Crystal structure of scapharca inaequivalvis hbi, I114F mutant ligated to carbon monoxide.
Analyse Crystal structure of scapharca inaequivalvis hbi, I114F mutant ligated to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JWN
- Type
- protein
- Length
- 580 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Globin I - ark shell
- UniProt
- P02213
- Ligands
- HEM, CMO
- Pockets
- 2 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Globin I - ark shell | protein | 145 | 84% helix, 0% strand | P02213 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- CMO · Carbon monoxide · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 945 | 0.87 | 0.88 | 68 | HEM, CMO |
| 2 | 933 | 0.87 | 0.88 | 66 | HEM, CMO |
Interfaces
2 interfaces between chains.
- A–B · 1014 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 979 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1JWN · Crystal Structure of Scapharca inaequivalvis HbI, I114F Mutant Ligated to Carbon Monoxide. · the same entry in another collection · chain D against D, TM-score 1.00
- P02213 · AlphaFold monomer V2.0 prediction for globin-1 (P02213) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P02213
- Elsewhere: RCSB PDB 1JWN · PDBe 1JWN · UniProt P02213
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