MolNFT v1 · #3599 · protein
Crystallization and X-ray structure determination of cytochrome C2 from rhodobacter sphaeroides in three crystal forms
1CXA: “Crystallization and X-ray structure determination of cytochrome C2 from rhodobacter sphaeroides in three…”. X-ray diffraction, 1 ligand (HEC), 1 pocket (best druggability 0.78). MolNFT v1 #3599 on GenesisL1: 3D structure, binding…
- PDB
- 1CXA
- Type
- protein
- Length
- 124 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C2
- UniProt
- P00095
- Ligands
- HEC
- Pockets
- 1 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C2 | protein | 124 | 40% helix, 6% strand | P00095 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.78 | 0.88 | 40 | IMD, HEC |
Modifications
Observed in the structure: 2 cofactor (heme c attachment).
Compared structures
- 1CXA · Crystallization and X-ray structure determination of cytochrome C2 from rhodobacter… · the same entry in another collection · chain A against A, TM-score 1.00
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 P00095
- Elsewhere: RCSB PDB 1CXA · PDBe 1CXA · UniProt P00095
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