Research workbench
Crystal structure of the carboxyl transferase subunit of putative pcc of sulfolobus tokodaii
Analyse Crystal structure of the carboxyl transferase subunit of putative pcc of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X0U
- Type
- protein
- Length
- 3,108 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical methylmalonyl-CoA decarboxylase alpha subunit
- UniProt
- Q974R9
- Pockets
- 20 · best druggability 0.84
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 | Hypothetical methylmalonyl-CoA decarboxylase alpha subunit | protein | 518 | 42% helix, 18% strand | Q974R9 |
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 | 862 | 0.84 | 0.86 | 89 | empty |
| 2 | 805 | 0.83 | 0.86 | 80 | empty |
| 3 | 798 | 0.83 | 0.86 | 69 | empty |
| 4 | 53 | 0.73 | 0.99 | 23 | empty |
| 5 | 52 | 0.72 | 0.99 | 22 | empty |
Interfaces
15 interfaces between chains.
- B–E · 5118 Ų buried · 68 hydrogen bonds · protein-protein
- A–D · 5075 Ų buried · 59 hydrogen bonds · protein-protein
- C–F · 4971 Ų buried · 62 hydrogen bonds · protein-protein
- B–C · 1509 Ų buried · 31 hydrogen bonds · protein-protein
- E–F · 1471 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 1X0U · Crystal Structure of the carboxyl transferase subunit of putative PCC of Sulfolobus… · 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 Q974R9
- Elsewhere: RCSB PDB 1X0U · PDBe 1X0U · UniProt Q974R9
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