Research workbench
Crystal structure of human acyl-CoA synthetase medium-chain family member 2A, with L64P mutation
Analyse Crystal structure of human acyl-CoA synthetase medium-chain family member 2A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B7W
- Type
- protein
- Length
- 537 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl-coenzyme a synthetase ACSM2A, mitochondrial precursor
- EC
- 6.2.1.2
- UniProt
- Q08AH3
- Ligands
- MG, CL
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyl-coenzyme a synthetase ACSM2A, mitochondrial precursor (EC 6.2.1.2) | protein | 537 | 32% helix, 26% strand | Q08AH3 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · 4 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 576 | 0.82 | 0.88 | 72 | CL |
| 2 | 263 | 0.54 | 0.76 | 32 | empty |
| 3 | 72 | 0.46 | 0.82 | 14 | empty |
| 4 | 99 | 0.45 | 0.80 | 23 | empty |
| 5 | 91 | 0.38 | 0.76 | 21 | empty |
Compared structures
- 3B7W · Crystal structure of human acyl-CoA synthetase medium-chain family member 2A, with L64P… · the same entry in another collection · chain A against A, TM-score 1.00
- Q08AH3 · AlphaFold monomer V2.0 prediction for acyl-coenzyme a synthetase ACSM2A, mitochondrial… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q08AH3
- Elsewhere: RCSB PDB 3B7W · PDBe 3B7W · UniProt Q08AH3
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