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Structure of the biotinyl domain of acetyl-coenzyme a carboxylase determined by mad phasing
Analyse Structure of the biotinyl domain of acetyl-coenzyme a carboxylase determined by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BDO
- Type
- protein
- Length
- 80 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA carboxylase
- EC
- 6.4.1.2
- UniProt
- P0ABD8
- Ligands
- BTN
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA carboxylase (EC 6.4.1.2) | protein | 80 | 0% helix, 45% strand | P0ABD8 |
Ligands and binding sites
- BTN · Biotin · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 cofactor (biotinylation).
Compared structures
- 1BDO · Structure of the biotinyl domain of acetyl-coenzyme a carboxylase determined by mad… · the same entry in another collection · chain A against A, TM-score 1.00
- P0ABD8 · AlphaFold monomer V2.0 prediction for biotin carboxyl carrier protein of acetyl-CoA… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P0ABD8
- Elsewhere: RCSB PDB 1BDO · PDBe 1BDO · UniProt P0ABD8
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