MolNFT v1 · #37112 · protein
Crystal structure of B. subtilis luxs in complex with (2S)-2-amino-4- [(2R,3R)-2,3-dihydroxy-3-N- hydroxycarbamoyl-PROPYLMERCAPTO]BUTYRIC acid
2FQO · S-ribosylhomocysteine lyase: “Crystal structure of B. subtilis luxs in complex with (2S)-2-amino-4- [(2R,3R)-2,3-dihydroxy-3-N…”. X-ray diffraction, 3 ligands (HYI, CO, SO4). MolNFT v1 #37112 on GenesisL1: 3D structure, binding…
- PDB
- 2FQO
- Type
- protein
- Length
- 154 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-ribosylhomocysteine lyase
- EC
- 4.4.1.21
- UniProt
- O34667
- Ligands
- HYI, CO, SO4
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-ribosylhomocysteine lyase (EC 4.4.1.21) | protein | 154 | 35% helix, 23% strand | O34667 |
Ligands and binding sites
- HYI · (2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoyl-propylmercapto]butyric acid · ligand · chains A
- CO · Cobalt (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 O34667
- Elsewhere: RCSB PDB 2FQO · PDBe 2FQO · UniProt O34667
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