MolNFT v1 · #118266 · protein
Crystal structure of the arabidopsis thaliana C-terminal chlh at 1.25A
5EWU · Magnesium-chelatase subunit chlh, chloroplastic: “Crystal structure of the arabidopsis thaliana C-terminal chlh at 1.25A”. X-ray diffraction, 2 ligands (BEZ, MG), 3 pockets (best druggability 0.79). MolNFT v1 #118266 on GenesisL1…
- PDB
- 5EWU
- Type
- protein
- Length
- 760 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Magnesium-chelatase subunit chlh, chloroplastic
- EC
- 6.6.1.1
- UniProt
- Q9FNB0
- Ligands
- BEZ, MG
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Magnesium-chelatase subunit chlh, chloroplastic (EC 6.6.1.1) | protein | 383 | 58% helix, 13% strand | Q9FNB0 |
| B | Magnesium-chelatase subunit chlh, chloroplastic (EC 6.6.1.1) | protein | 377 | 56% helix, 13% strand | Q9FNB0 |
Ligands and binding sites
- BEZ · Benzoic acid · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 924 | 0.79 | 0.82 | 92 | empty |
| 2 | 151 | 0.49 | 0.78 | 36 | BEZ, MG |
| 3 | 119 | 0.47 | 0.79 | 29 | BEZ, MG |
Interfaces
1 interface between chains.
- A–B · 802 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5EWU · Crystal structure of the Arabidopsis thaliana C-terminal Chlh at 1.25A · the same entry in another collection · chain A against A, TM-score 1.00
- Q9FNB0 · AlphaFold monomer V2.0 prediction for magnesium-chelatase subunit chlh, chloroplastic… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9FNB0
- Elsewhere: RCSB PDB 5EWU · PDBe 5EWU · UniProt Q9FNB0
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