MolNFT v1 · #69620 · protein
Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA flk - T42S mutant in complex with acetyl-CoA
3KVU: “Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA flk - T42S mutant in…”. X-ray diffraction. MolNFT v1 #69620 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3KVU
- Type
- protein
- Length
- 532 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q1EMV2
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 133 | — | Q1EMV2 |
Compared structures
- 3KVU · Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA FlK… · the same entry in another collection · chain C against C, TM-score 1.00
- Q1EMV2 · AlphaFold monomer V2.0 prediction for fluoroacetyl-CoA thioesterase (Q1EMV2) · a predicted model of the same protein · chain D 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 Q1EMV2
- Elsewhere: RCSB PDB 3KVU · PDBe 3KVU · UniProt Q1EMV2
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