Research workbench
Crystal structure of SFYFP66BPAC203Y
Analyse Crystal structure of SFYFP66BPAC203Y in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L02
- Type
- protein
- Length
- 227 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A059PIR9
- Ligands
- BF6
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 227 | — | A0A059PIR9 |
Ligands and binding sites
- BF6 · [(4Z)-2-(aminomethyl)-4-{[4-(benzenecarbonyl) phenyl]methylidene}-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6L02 · Crystal Structure of sfYFP66BPAC203Y · 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 A0A059PIR9
- Elsewhere: RCSB PDB 6L02 · PDBe 6L02 · UniProt A0A059PIR9
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