Research workbench
Structure of reductive aminase from aspergillus terreus in complex with NADPH
Analyse Structure of reductive aminase from aspergillus terreus in complex with NADPH in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EOD
- Type
- protein
- Length
- 2,216 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q0CCT3
- Ligands
- NAP
Structure
x-ray diffraction · 8 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 285 | — | Q0CCT3 |
| B | — | protein | 284 | — | Q0CCT3 |
| C | — | protein | 279 | — | Q0CCT3 |
| D | — | protein | 279 | — | Q0CCT3 |
| F | — | protein | 262 | — | Q0CCT3 |
| G | — | protein | 263 | — | Q0CCT3 |
| E | — | protein | 283 | — | Q0CCT3 |
| H | — | protein | 281 | — | Q0CCT3 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 3 copies · chains A, H, B, G, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6EOD · Structure of Reductive Aminase from Aspergillus terreus in complex with NADPH · the same entry in another collection · chain C against C, 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 Q0CCT3
- Elsewhere: RCSB PDB 6EOD · PDBe 6EOD · UniProt Q0CCT3
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