Research workbench
Structure of the 2-octenoyl-CoA carboxylase reductase cinf in complex with NADP and 2-octenoyl-CoA
Analyse Structure of the 2-octenoyl-CoA carboxylase reductase cinf 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
- 4A0S
- Type
- protein
- Length
- 1,778 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Octenoyl-CoA REDUCTASE/CARBOXYLASE
- UniProt
- F0V3Z3
- Ligands
- CO8, NAP
- Pockets
- 12 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Octenoyl-CoA REDUCTASE/CARBOXYLASE | protein | 445 | 37% helix, 21% strand | F0V3Z3 |
| C, D | Octenoyl-CoA REDUCTASE/CARBOXYLASE | protein | 444 | 35% helix, 21% strand | F0V3Z3 |
Ligands and binding sites
- CO8 · Octanoyl-coenzyme A · ligand · 4 copies · chains A, D, B, C
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 759 | 0.82 | 0.85 | 74 | NAP, CO8 |
| 2 | 742 | 0.81 | 0.84 | 72 | NAP, CO8 |
| 3 | 841 | 0.80 | 0.83 | 76 | CO8, NAP |
| 4 | 851 | 0.80 | 0.82 | 73 | NAP, CO8 |
| 5 | 88 | 0.77 | 0.99 | 19 | empty |
Interfaces
6 interfaces between chains.
- B–C · 1555 Ų buried · 34 hydrogen bonds · protein-protein
- A–D · 1529 Ų buried · 36 hydrogen bonds · protein-protein
- A–B · 1294 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 1293 Ų buried · 32 hydrogen bonds · protein-protein
- B–D · 654 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 4A0S · Structure of the 2-octenoyl-CoA carboxylase reductase cinf in complex with NADP and… · 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 F0V3Z3
- Elsewhere: RCSB PDB 4A0S · PDBe 4A0S · UniProt F0V3Z3
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