Research workbench
Structure of cytochrome F from chlamydomonas reinhardtii
Analyse Structure of cytochrome F from chlamydomonas reinhardtii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EWH
- Type
- protein
- Length
- 753 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome F
- UniProt
- P23577
- Ligands
- HEC
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Cytochrome F | protein | 251 | 10% helix, 37% strand | P23577 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1189 | 0.82 | 0.83 | 136 | HEC |
| 2 | 169 | 0.70 | 0.88 | 36 | HEC |
| 3 | 69 | 0.33 | 0.75 | 13 | empty |
| 4 | 57 | 0.33 | 0.76 | 12 | empty |
| 5 | 53 | 0.30 | 0.75 | 12 | empty |
Interfaces
2 interfaces between chains.
- A–C · 465 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 156 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 cofactor (heme c attachment).
Compared structures
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 P23577
- Elsewhere: RCSB PDB 1EWH · PDBe 1EWH · UniProt P23577
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