Research workbench
Joint-functions of protein residues and NADP(H) in oxygen-activation by flavin-containing monooxygenase: complex with 3-acetylpyridine adenine dinucleotide phosphate (apadp)
Analyse Joint-functions of protein residues and NADP(H) in oxygen-activation by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XLT
- Type
- protein
- Length
- 1,784 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q83XK4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 446 | — | Q83XK4 |
Compared structures
- 2XLT · Joint-functions of protein residues and NADP(H) in oxygen-activation by flavin-containing… · 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 Q83XK4
- Elsewhere: RCSB PDB 2XLT · PDBe 2XLT · UniProt Q83XK4
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