MolNFT v1 · #166095 · protein
Structure of proline utilization a with the FAD covalently modified by L-thiazolidine-2-carboxylate and three cysteines (CYS46, CYS470, CYS638) modified to S,S-(2-HYDROXYETHYL)THIOCYSTEINE
6UFP: “Structure of proline utilization a with the FAD covalently modified by L-thiazolidine-2-carboxylate and three…”. X-ray diffraction, 4 ligands (FDA, T2C, NAD). MolNFT v1 #166095 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6UFP
- Type
- protein
- Length
- 2,394 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- F7X6I3
- Ligands
- FDA, T2C, NAD, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1197 | — | F7X6I3 |
| B | — | protein | 1197 | — | F7X6I3 |
Ligands and binding sites
- FDA · Dihydroflavine-adenine dinucleotide · ligand · 2 copies · chains A, B
- T2C · (2S)-1,3-thiazolidine-2-carboxylic acid · ligand · 2 copies · chains A, B
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
- FMT · Formic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UFP · Structure of proline utilization A with the FAD covalently modified by… · 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 F7X6I3
- Elsewhere: RCSB PDB 6UFP · PDBe 6UFP · UniProt F7X6I3
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