Research workbench
Coproporphyrinogen III oxidase (hemn) from escherichia COLI is a radical SAM enzyme.
Analyse Coproporphyrinogen III oxidase (hemn) from escherichia COLI is a radical SAM… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OLT
- Type
- protein
- Length
- 434 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oxygen-independent coproporphyrinogen III oxidase
- EC
- 1.3.-.-
- UniProt
- P32131
- Ligands
- SAM, SF4
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxygen-independent coproporphyrinogen III oxidase (EC 1.3.-.-) | protein | 434 | 42% helix, 21% strand | P32131 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · 2 copies · chains A
- SF4 · Iron/sulfur cluster · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 967 | 0.84 | 0.85 | 92 | SF4, SAM |
| 2 | 178 | 0.50 | 0.77 | 21 | empty |
| 3 | 83 | 0.35 | 0.76 | 19 | empty |
| 4 | 65 | 0.34 | 0.76 | 16 | empty |
Compared structures
- 1OLT · Coproporphyrinogen III oxidase (HemN) from Escherichia coli is a Radical SAM enzyme. · the same entry in another collection · chain A against A, TM-score 1.00
- P32131 · AlphaFold monomer V2.0 prediction for oxygen-independent coproporphyrinogen III oxidase… · 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 P32131
- Elsewhere: RCSB PDB 1OLT · PDBe 1OLT · UniProt P32131
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.