Research workbench
Propionibacterium shermanii transcarboxylase 5S subunit bound to pyruvic acid
Analyse Propionibacterium shermanii transcarboxylase 5S subunit bound to pyruvic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RQH
- Type
- protein
- Length
- 471 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcarboxylase 5S subunit
- EC
- 2.1.3.1
- Ligands
- PYR, CO
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcarboxylase 5S subunit (EC 2.1.3.1) | protein | 471 | 50% helix, 10% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 566 | 0.68 | 0.78 | 62 | PYR |
| 2 | 115 | 0.46 | 0.78 | 15 | empty |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 1RQH · Propionibacterium shermanii transcarboxylase 5S subunit bound to pyruvic acid · 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 1RQH · PDBe 1RQH
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