MolNFT v1 · #165647 · protein
Crystal structure of acyl-ACP/ACYL-CoA dehydrogenase from allylmalonyl-CoA and FK506 biosynthesis, tcsd
6U1V: “Crystal structure of acyl-ACP/ACYL-CoA dehydrogenase from allylmalonyl-CoA and FK506 biosynthesis, tcsd”. X-ray diffraction, 1 ligand (FDA). MolNFT v1 #165647 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6U1V
- Type
- protein
- Length
- 1,542 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- I2MTW3
- Ligands
- FDA
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 388 | — | I2MTW3 |
| B | — | protein | 389 | — | I2MTW3 |
| C | — | protein | 383 | — | I2MTW3 |
| D | — | protein | 382 | — | I2MTW3 |
Ligands and binding sites
- FDA · Dihydroflavine-adenine dinucleotide · ligand · 4 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6U1V · Crystal structure of acyl-ACP/acyl-CoA dehydrogenase from allylmalonyl-CoA and FK506… · 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 I2MTW3
- Elsewhere: RCSB PDB 6U1V · PDBe 6U1V · UniProt I2MTW3
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