MolNFT v1 · #1116 · protein
Crystal structure of the fungal peroxidase from arthromyces ramosus at 1.9 ångströms resolution: structural comparisons with the lignin and cytochrome C peroxidases
1ARP: “Crystal structure of the fungal peroxidase from arthromyces ramosus at 1.9 ångströms resolution: structural…”. X-ray diffraction, 3 ligands (HEM, NAG, CA), 1 pocket (best druggability 0.80). MolNFT v1 #1116 on GenesisL1: 3D…
- PDB
- 1ARP
- Type
- protein
- Length
- 336 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxidase
- EC
- 1.11.1.7
- UniProt
- P28313
- Ligands
- HEM, NAG, CA
- Pockets
- 1 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxidase (EC 1.11.1.7) | protein | 336 | 44% helix, 7% strand | P28313 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 406 | 0.80 | 0.88 | 40 | HEM |
Modifications
Observed in the structure: 4 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 1ARP · Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 angstroms… · the same entry in another collection · chain A against A, TM-score 1.00
- P28313 · AlphaFold monomer V2.0 prediction for peroxidase (P28313) · 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 P28313
- Elsewhere: RCSB PDB 1ARP · PDBe 1ARP · UniProt P28313
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