Research workbench
Crystal structure of FMN-dependent cysteine decarboxylases spaf
Analyse Crystal structure of FMN-dependent cysteine decarboxylases spaf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CFU
- Type
- protein
- Length
- 4,201 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1R1S5L5
- Ligands
- FMN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F, H, P, A, B, C, D, E, G, I, J, K, L, M, N, O, Q, R, T, U, V, W, X | — | protein | 175 | — | A0A1R1S5L5 |
| S | — | protein | 176 | — | A0A1R1S5L5 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 24 copies · chains F, H, D, S, L, T, P, N, A, B, I, C, W, E, G, M, U, J, K, X, O, Q, R, V
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7CFU · Crystal Structure of FMN-dependent Cysteine Decarboxylases SpaF · the same entry in another collection · chain X against X, 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 A0A1R1S5L5
- Elsewhere: RCSB PDB 7CFU · PDBe 7CFU · UniProt A0A1R1S5L5
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