Research workbench
Structure of crotonyl-CoA CARBOXYLASE/REDUCTASE ante in complex with NADP
Analyse Structure of crotonyl-CoA CARBOXYLASE/REDUCTASE ante in complex with NADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Y0K
- Type
- protein
- Length
- 405 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ante
- UniProt
- M1SQA1
- Ligands
- NAP
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ante | protein | 405 | 33% helix, 22% strand | M1SQA1 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 637 | 0.76 | 0.82 | 54 | NAP |
| 2 | 83 | 0.37 | 0.77 | 20 | empty |
| 3 | 75 | 0.35 | 0.76 | 16 | empty |
Compared structures
- 4Y0K · Structure of crotonyl-CoA carboxylase/reductase AntE in complex with NADP · 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 M1SQA1
- Elsewhere: RCSB PDB 4Y0K · PDBe 4Y0K · UniProt M1SQA1
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