Research workbench
LARC2, the C-terminal domain of a cyclometallase involved in the synthesis of the npn cofactor of lactate racemase, in complex with mnctp
Analyse LARC2, the C-terminal domain of a cyclometallase involved in the synthesis of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BWQ
- Type
- protein
- Length
- 286 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel insertion protein
- UniProt
- F9UST1
- Ligands
- CTP, MN, CL
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel insertion protein | protein | 144 | 35% helix, 44% strand | F9UST1 |
| B | Pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel insertion protein | protein | 142 | 36% helix, 40% strand | F9UST1 |
Ligands and binding sites
- CTP · Cytidine-5'-triphosphate · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 6 copies · chains A, B
- CL · Chloride ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 812 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6BWQ · LarC2, the C-terminal domain of a cyclometallase involved in the synthesis of the NPN… · the same entry in another collection · chain A against A, TM-score 1.00
- F9UST1 · AlphaFold monomer V2.0 prediction for pyridinium-3,5-bisthiocarboxylic acid… · a predicted model of the same protein · chain B against A, TM-score 0.91
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 F9UST1
- Elsewhere: RCSB PDB 6BWQ · PDBe 6BWQ · UniProt F9UST1
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