Research workbench
Cytochrome C557: improperly folded thermus thermophilus C552
Analyse Cytochrome C557: improperly folded thermus thermophilus C552 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FOC
- Type
- protein
- Length
- 256 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome RC557
- UniProt
- P04164
- Ligands
- HEC
- Pockets
- 2 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytochrome RC557 | protein | 128 | 36% helix, 5% strand | P04164 |
Ligands and binding sites
- HEC · Heme C · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 739 | 0.87 | 0.90 | 88 | HEC |
| 2 | 61 | 0.28 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 469 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor, 1 disulfide (heme c attachment, disulfide).
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 P04164
- Elsewhere: RCSB PDB 1FOC · PDBe 1FOC · UniProt P04164
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.