Research workbench
Solution structure of B domain from human propionyl-CoA carboxylase alpha subunit
Analyse Solution structure of B domain from human propionyl-CoA carboxylase alpha… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CQY
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- EC
- 6.4.1.3
- UniProt
- P05165
- Pockets
- 1 · best druggability 0.32
Structure
solution nmr · 1 distinct chain · 27% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Propionyl-CoA carboxylase alpha chain, mitochondrial (EC 6.4.1.3) | protein | 108 | 27% helix, 13% strand | P05165 |
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 | 68 | 0.32 | 0.75 | 21 | empty |
Compared structures
- 2CQY · Solution structure of B domain from human propionyl-CoA carboxylase alpha subunit · the same entry in another collection · chain A against A, TM-score 1.00
- P05165 · AlphaFold monomer V2.0 prediction for propionyl-CoA carboxylase alpha chain… · a predicted model of the same protein · chain A against A, TM-score 0.63
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 P05165
- Elsewhere: RCSB PDB 2CQY · PDBe 2CQY · UniProt P05165
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