MolNFT v1 · #169352 · protein
Structure of proline utilization a with D-proline bound in the L- glutamate-gamma-semialdehyde dehydrogenase active site
6X99: “Structure of proline utilization a with D-proline bound in the L- glutamate-gamma-semialdehyde dehydrogenase…”. X-ray diffraction, 2 ligands (FAD, SO4). MolNFT v1 #169352 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6X99
- Type
- protein
- Length
- 2,433 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- F7X6I3
- Ligands
- FAD, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1218 | — | F7X6I3 |
| B | — | protein | 1215 | — | F7X6I3 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 9 copies · chains A, B
- PGE · Triethylene glycol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6X99 · Structure of proline utilization A with D-proline bound in the… · the same entry in another collection · chain B against B, 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 6X99 · PDBe 6X99 · UniProt F7X6I3
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