Research workbench
Crystal structure of the streptomyces coelicolor H110A acps mutant in complex with cofactor CoA at 1.3 a
Analyse Crystal structure of the streptomyces coelicolor H110A acps mutant in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WDS
- Type
- protein
- Length
- 123 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Holo-[acyl-carrier-protein] synthase
- EC
- 2.7.8.7
- UniProt
- O86785
- Ligands
- COA, MG
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Holo-[acyl-carrier-protein] synthase (EC 2.7.8.7) | protein | 123 | 40% helix, 33% strand | O86785 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2WDS · Crystal structure of the Streptomyces coelicolor H110A AcpS mutant in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- O86785 · AlphaFold monomer V2.0 prediction for holo-[acyl-carrier-protein] synthase (O86785) · a predicted model of the same protein · 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
- Every structure of UniProt O86785
- Elsewhere: RCSB PDB 2WDS · PDBe 2WDS · UniProt O86785
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