MolNFT v1 · #98739 · protein
Crystal structure of an apoptosis-inducing factor, mitochondrion- associated, 1 (AIFM1) from homo sapiens at 1.88 a resolution
4LII · Apoptosis-inducing factor 1, mitochondrial: “Crystal structure of an apoptosis-inducing factor, mitochondrion- associated, 1 (AIFM1) from homo sapiens at…”. X-ray diffraction, 1 ligand (FAD), 3 pockets (best druggability 0.82).…
- PDB
- 4LII
- Type
- protein
- Length
- 474 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apoptosis-inducing factor 1, mitochondrial
- EC
- 1.-.-.-
- UniProt
- O95831
- Ligands
- FAD
- Pockets
- 3 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Apoptosis-inducing factor 1, mitochondrial (EC 1.-.-.-) | protein | 474 | 28% helix, 29% strand | O95831 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
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 | 1026 | 0.82 | 0.83 | 88 | FAD, EDO |
| 2 | 91 | 0.40 | 0.77 | 19 | empty |
| 3 | 79 | 0.32 | 0.74 | 16 | empty |
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 4LII · Crystal structure of an apoptosis-inducing factor, mitochondrion-associated, 1 (AIFM1)… · the same entry in another collection · chain A against A, TM-score 1.00
- O95831 · AlphaFold monomer V2.0 prediction for apoptosis-inducing factor 1, mitochondrial (O95831) · a predicted model of the same protein · 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 O95831
- Elsewhere: RCSB PDB 4LII · PDBe 4LII · UniProt O95831
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