Research workbench
Crystal structure of P. aeruginosa geranyl-CoA carboxylase (gcc), beta subunit
Analyse Crystal structure of P. aeruginosa geranyl-CoA carboxylase (gcc), beta subunit in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5IKL
- Type
- protein
- Length
- 1,486 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Geranyl-CoA carboxylase, beta-subunit
- UniProt
- Q9HZV9
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Geranyl-CoA carboxylase, beta-subunit | protein | 514 | 46% helix, 18% strand | Q9HZV9 |
| D | Geranyl-CoA carboxylase, beta-subunit | protein | 512 | 45% helix, 18% strand | Q9HZV9 |
| F | Geranyl-CoA carboxylase, beta-subunit | protein | 460 | 42% helix, 19% strand | Q9HZV9 |
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 383 | 0.80 | 0.89 | 44 | empty |
| 2 | 392 | 0.79 | 0.88 | 38 | empty |
| 3 | 428 | 0.74 | 0.84 | 44 | empty |
| 4 | 528 | 0.65 | 0.77 | 67 | empty |
| 5 | 315 | 0.60 | 0.78 | 48 | empty |
Interfaces
3 interfaces between chains.
- B–D · 1338 Ų buried · 14 hydrogen bonds · protein-protein
- D–F · 1312 Ų buried · 11 hydrogen bonds · protein-protein
- B–F · 1251 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 5IKL · Crystal structure of P. aeruginosa geranyl-CoA carboxylase (GCC), beta subunit · the same entry in another collection · chain B against B, 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 Q9HZV9
- Elsewhere: RCSB PDB 5IKL · PDBe 5IKL · UniProt Q9HZV9
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