Research workbench
Crystal structure of the carboxyltransferase subunit of acc from staphylococcus aureus
Analyse Crystal structure of the carboxyltransferase subunit of acc from staphylococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F9I
- Type
- protein
- Length
- 1,121 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-coenzyme a carboxylase carboxyl transferase subunit alpha; Acetyl-coenzyme a…
- Ligands
- ZN
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-coenzyme a carboxylase carboxyl transferase subunit alpha | protein | 309 | 50% helix, 17% strand | — |
| B | Acetyl-coenzyme a carboxylase carboxyl transferase subunit beta | protein | 260 | 39% helix, 22% strand | — |
| C | Acetyl-coenzyme a carboxylase carboxyl transferase subunit alpha | protein | 297 | 49% helix, 17% strand | — |
| D | Acetyl-coenzyme a carboxylase carboxyl transferase subunit beta | protein | 255 | 40% helix, 22% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1153 | 0.79 | 0.80 | 60 | empty |
| 2 | 574 | 0.71 | 0.80 | 62 | empty |
| 3 | 541 | 0.69 | 0.79 | 60 | empty |
| 4 | 205 | 0.55 | 0.78 | 35 | empty |
| 5 | 147 | 0.48 | 0.78 | 24 | empty |
Interfaces
5 interfaces between chains.
- C–D · 2334 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 2321 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 944 Ų buried · 24 hydrogen bonds · protein-protein
- A–D · 924 Ų buried · 25 hydrogen bonds · protein-protein
- A–C · 313 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2F9I · Crystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureus · 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
- Elsewhere: RCSB PDB 2F9I · PDBe 2F9I
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