Research workbench
Crystal structure of human apoptosis-inducing factor with W196A mutation
Analyse Crystal structure of human apoptosis-inducing factor with W196A mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KVH
- Type
- protein
- Length
- 876 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apoptosis-inducing factor 1, mitochondrial
- EC
- 1.1.1.-
- UniProt
- O95831
- Ligands
- FAD
- Pockets
- 9 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Apoptosis-inducing factor 1, mitochondrial (EC 1.1.1.-) | protein | 438 | 26% helix, 32% strand | O95831 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1051 | 0.82 | 0.83 | 101 | FAD |
| 2 | 1037 | 0.82 | 0.83 | 97 | FAD |
| 3 | 87 | 0.75 | 0.97 | 27 | empty |
| 4 | 167 | 0.44 | 0.74 | 24 | empty |
| 5 | 83 | 0.34 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 707 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 5KVH · Crystal structure of human apoptosis-inducing factor with W196A mutation · 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 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 O95831
- Elsewhere: RCSB PDB 5KVH · PDBe 5KVH · UniProt O95831
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