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Crystal structure of pyruvate oxidoreductase subunit porc (ec 1.2.7.1) (TM0015) from thermotoga maritima at 2.12 a resolution
Analyse Crystal structure of pyruvate oxidoreductase subunit porc (ec 1.2.7.1) (TM0015)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RAA
- Type
- protein
- Length
- 178 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyruvate synthase subunit porc
- EC
- 1.2.7.1
- UniProt
- O05650
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyruvate synthase subunit porc (EC 1.2.7.1) | protein | 178 | 43% helix, 22% strand | O05650 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.31 | 0.75 | 12 | empty |
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 2RAA · Crystal structure of pyruvate oxidoreductase subunit PORC (EC 1.2.7.1) (TM0015) from… · the same entry in another collection · chain A against A, TM-score 1.00
- O05650 · AlphaFold monomer V2.0 prediction for pyruvate synthase subunit porc (O05650) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O05650
- Elsewhere: RCSB PDB 2RAA · PDBe 2RAA · UniProt O05650
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