Research workbench
Structure of active cystathionine B-synthase from apis mellifera
Analyse Structure of active cystathionine B-synthase from apis mellifera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OHX
- Type
- protein
- Length
- 976 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q2V0C9
- Ligands
- HEM, PLP
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 488 | — | Q2V0C9 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OHX · Structure of active cystathionine B-synthase from Apis mellifera · the same entry in another collection · chain A against A, TM-score 1.00
- Q2V0C9 · AlphaFold monomer V2.0 prediction for cystathionine beta-synthase (Q2V0C9) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 Q2V0C9
- Elsewhere: RCSB PDB 5OHX · PDBe 5OHX · UniProt Q2V0C9
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