MolNFT v1 · #122971 · protein
Crystal structure of AFMP4P in complex with arachidonic acid
5J5L · Uncharacterized protein: “Crystal structure of AFMP4P in complex with arachidonic acid”. X-ray diffraction, 1 ligand (ACD), 1 pocket (best druggability 0.81). MolNFT v1 #122971 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 5J5L
- Type
- protein
- Length
- 152 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q4WZA5
- Ligands
- ACD
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 88% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 152 | 88% helix, 0% strand | Q4WZA5 |
Ligands and binding sites
- ACD · Arachidonic acid · 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 | 176 | 0.81 | 0.96 | 30 | ACD |
Compared structures
- 5J5L · Crystal structure of AFMP4P in complex with arachidonic acid · 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 Q4WZA5
- Elsewhere: RCSB PDB 5J5L · PDBe 5J5L · UniProt Q4WZA5
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