Research workbench
Crystal structure of fatty acid amide hydrolase
Analyse Crystal structure of fatty acid amide hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MT5
- Type
- protein
- Length
- 8,592 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty-acid amide hydrolase
- EC
- 3.1.-.-
- UniProt
- P97612
- Ligands
- MAY
- Pockets
- 20 · best druggability 0.90
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P | Fatty-acid amide hydrolase (EC 3.1.-.-) | protein | 537 | 44% helix, 12% strand | P97612 |
Ligands and binding sites
- MAY · Methyl arachidonyl fluorophosphonate · ligand · 16 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1086 | 0.90 | 0.92 | 123 | MAY |
| 2 | 1143 | 0.90 | 0.92 | 133 | MAY |
| 3 | 1144 | 0.90 | 0.91 | 130 | MAY |
| 4 | 883 | 0.89 | 0.91 | 96 | MAY |
| 5 | 636 | 0.89 | 0.93 | 91 | MAY |
Interfaces
26 interfaces between chains.
- A–B · 1650 Ų buried · 15 hydrogen bonds · protein-protein
- K–L · 1647 Ų buried · 16 hydrogen bonds · protein-protein
- E–F · 1631 Ų buried · 15 hydrogen bonds · protein-protein
- O–P · 1622 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1622 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 covalent (covalent ligand).
Compared structures
- 1MT5 · Crystal structure of fatty acid amide hydrolase · the same entry in another collection · chain J against J, 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 P97612
- Elsewhere: RCSB PDB 1MT5 · PDBe 1MT5 · UniProt P97612
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.