MolNFT v1 · #120712 · protein
Crystal structure of the C49A C353A mutant fenna-matthews-olson protein from chlorobaculum tepidum
5H8Z · Bacteriochlorophyll a protein: “Crystal structure of the C49A C353A mutant fenna-matthews-olson protein from chlorobaculum tepidum”. X-ray diffraction, 1 ligand (BCL), 8 pockets (best druggability 0.81). MolNFT v1 #120712 on…
- PDB
- 5H8Z
- Type
- protein
- Length
- 716 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacteriochlorophyll a protein
- UniProt
- Q46393
- Ligands
- BCL
- Pockets
- 8 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Bacteriochlorophyll a protein | protein | 358 | 17% helix, 50% strand | Q46393 |
Ligands and binding sites
- BCL · Bacteriochlorophyll A · ligand · 16 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1056 | 0.81 | 0.82 | 111 | BCL |
| 2 | 561 | 0.78 | 0.84 | 77 | BCL |
| 3 | 170 | 0.64 | 0.84 | 26 | BCL |
| 4 | 220 | 0.64 | 0.82 | 27 | BCL |
| 5 | 208 | 0.55 | 0.79 | 27 | empty |
Interfaces
1 interface between chains.
- A–C · 244 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5H8Z · Crystal structure of the C49A C353A mutant Fenna-Matthews-Olson Protein from… · the same entry in another collection · chain A against A, TM-score 1.00
- Q46393 · AlphaFold monomer V2.0 prediction for bacteriochlorophyll a protein (Q46393) · a predicted model of the same protein · chain C 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 Q46393
- Elsewhere: RCSB PDB 5H8Z · PDBe 5H8Z · UniProt Q46393
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