MolNFT v1 · #143904 · protein
Crystal structure of FE(II) unliganded H-nox protein from K. algicida
6BDD · 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase: “Crystal structure of FE(II) unliganded H-nox protein from K. algicida”. X-ray diffraction, 1 ligand (HEM), 1 pocket (best druggability 0.84). MolNFT v1 #143904 on GenesisL1: 3D…
- PDB
- 6BDD
- Type
- protein
- Length
- 185 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase
- UniProt
- A9DSJ8
- Ligands
- HEM
- Pockets
- 1 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase | protein | 185 | 51% helix, 18% strand | A9DSJ8 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
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 | 368 | 0.84 | 0.92 | 36 | HEM |
Compared structures
- 6BDD · Crystal structure of Fe(II) unliganded H-NOX protein from K. algicida · 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 A9DSJ8
- Elsewhere: RCSB PDB 6BDD · PDBe 6BDD · UniProt A9DSJ8
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