MolNFT v1 · #18279 · protein
Structure and function of cysg, the multifunctional METHYLTRANSFERASE/DEHYDROGENASE/FERROCHELATASE for siroheme synthesis
1PJQ · Siroheme synthase: “Structure and function of cysg, the multifunctional METHYLTRANSFERASE/DEHYDROGENASE/FERROCHELATASE for…”. X-ray diffraction, 1 ligand (SAH), 12 pockets (best druggability 0.77). MolNFT v1 #18279 on GenesisL1: 3D…
- PDB
- 1PJQ
- Type
- protein
- Length
- 903 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Siroheme synthase
- EC
- 2.1.1.107, 1.-.-.-, 4.99.1.-
- UniProt
- P25924
- Ligands
- SAH
- Pockets
- 12 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Siroheme synthase (EC 2.1.1.107, 1.-.-.-, 4.99.1.-) | protein | 448 | 38% helix, 22% strand | P25924 |
| B | Siroheme synthase (EC 2.1.1.107, 1.-.-.-, 4.99.1.-) | protein | 455 | 38% helix, 22% strand | P25924 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains B
- ACT · Acetate ion · additive · 3 copies · chains A, B
- PGE · Triethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1073 | 0.77 | 0.79 | 96 | ACT |
| 2 | 376 | 0.72 | 0.84 | 51 | PGE |
| 3 | 621 | 0.72 | 0.79 | 51 | SAH |
| 4 | 471 | 0.69 | 0.80 | 61 | ACT |
| 5 | 241 | 0.59 | 0.80 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 6378 Ų buried · 96 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
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 P25924
- Elsewhere: RCSB PDB 1PJQ · PDBe 1PJQ · UniProt P25924
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