Research workbench
Crystal structure of biotin carboxylase from pseudomonas aeruginosa in apo form
Analyse Crystal structure of biotin carboxylase from pseudomonas aeruginosa in apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C00
- Type
- protein
- Length
- 879 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biotin carboxylase
- EC
- 6.3.4.14
- UniProt
- P37798
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biotin carboxylase (EC 6.3.4.14) | protein | 440 | 35% helix, 27% strand | P37798 |
| B | Biotin carboxylase (EC 6.3.4.14) | protein | 439 | 35% helix, 27% strand | P37798 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 471 | 0.73 | 0.83 | 53 | empty |
| 2 | 64 | 0.68 | 0.95 | 29 | empty |
| 3 | 468 | 0.62 | 0.76 | 54 | SO4 |
| 4 | 288 | 0.56 | 0.76 | 39 | SO4 |
| 5 | 179 | 0.46 | 0.75 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 1320 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 2C00 · Crystal Structure of Biotin Carboxylase from Pseudomonas aeruginosa in apo form · the same entry in another collection · chain A against A, TM-score 1.00
- P37798 · AlphaFold monomer V2.0 prediction for biotin carboxylase (P37798) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 P37798
- Elsewhere: RCSB PDB 2C00 · PDBe 2C00 · UniProt P37798
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