Research workbench
Solution structure of biotinoyl domain from human acetyl-CoA carboxylase 2
Analyse Solution structure of biotinoyl domain from human acetyl-CoA carboxylase 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KCC
- Type
- protein
- Length
- 84 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA carboxylase 2
- EC
- 6.4.1.2, 6.3.4.14
- UniProt
- O00763
Structure
solution nmr · 1 distinct chain · 0% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA carboxylase 2 (EC 6.4.1.2, 6.3.4.14) | protein | 84 | 0% helix, 35% strand | O00763 |
Compared structures
- 2KCC · Solution Structure of biotinoyl domain from human acetyl-CoA carboxylase 2 · the same entry in another collection · chain A against A, TM-score 1.00
- O00763 · AlphaFold monomer V2.0 prediction for acetyl-CoA carboxylase 2 (O00763) · a predicted model of the same protein · chain A against A, TM-score 0.81
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 O00763
- Elsewhere: RCSB PDB 2KCC · PDBe 2KCC · UniProt O00763
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