Research workbench
Acyl-CoA carboxylase beta subunit from S. coelicolor (pccb), apo form #2, mutant D422I
Analyse Acyl-CoA carboxylase beta subunit from S. coelicolor (pccb), apo form #2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XNW
- Type
- protein
- Length
- 3,126 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Propionyl-CoA carboxylase complex B subunit
- EC
- 6.4.1.3
- UniProt
- Q9X4K7
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Propionyl-CoA carboxylase complex B subunit (EC 6.4.1.3) | protein | 521 | 42% helix, 18% strand | Q9X4K7 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1135 | 0.80 | 0.82 | 94 | empty |
| 2 | 1186 | 0.80 | 0.82 | 105 | empty |
| 3 | 1125 | 0.80 | 0.81 | 74 | empty |
| 4 | 1113 | 0.76 | 0.79 | 127 | empty |
| 5 | 63 | 0.73 | 0.98 | 26 | empty |
Interfaces
15 interfaces between chains.
- B–E · 4824 Ų buried · 60 hydrogen bonds · protein-protein
- C–F · 4793 Ų buried · 65 hydrogen bonds · protein-protein
- A–D · 4782 Ų buried · 62 hydrogen bonds · protein-protein
- A–C · 1458 Ų buried · 18 hydrogen bonds · protein-protein
- D–F · 1456 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 1XNW · Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #2, mutant D422I · 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 Q9X4K7
- Elsewhere: RCSB PDB 1XNW · PDBe 1XNW · UniProt Q9X4K7
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