Research workbench
Crystal structure of the acyl-CoA carboxylase, ACCD5, from mycobacterium tuberculosis
Analyse Crystal structure of the acyl-CoA carboxylase, ACCD5, from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A7S
- Type
- protein
- Length
- 3,174 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable propionyl-CoA carboxylase beta chain 5
- EC
- 6.4.1.3
- UniProt
- P96885
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Probable propionyl-CoA carboxylase beta chain 5 (EC 6.4.1.3) | protein | 529 | 40% helix, 17% strand | P96885 |
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 | 944 | 0.83 | 0.85 | 99 | empty |
| 2 | 900 | 0.83 | 0.85 | 98 | empty |
| 3 | 1098 | 0.82 | 0.83 | 107 | empty |
| 4 | 65 | 0.75 | 0.99 | 24 | empty |
| 5 | 668 | 0.74 | 0.80 | 75 | empty |
Interfaces
14 interfaces between chains.
- C–F · 4872 Ų buried · 69 hydrogen bonds · protein-protein
- B–E · 4864 Ų buried · 64 hydrogen bonds · protein-protein
- A–D · 4853 Ų buried · 69 hydrogen bonds · protein-protein
- A–C · 1474 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 1451 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2A7S · Crystal Structure of the Acyl-CoA Carboxylase, AccD5, from Mycobacterium tuberculosis · 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 P96885
- Elsewhere: RCSB PDB 2A7S · PDBe 2A7S · UniProt P96885
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