MolNFT v1 · #14889 · protein
Manganese peroxidase
1MNP: “Manganese peroxidase”. X-ray diffraction, 4 ligands (HEM, NAG, CA), 3 pockets (best druggability 0.80). MolNFT v1 #14889 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MNP
- Type
- protein
- Length
- 357 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Manganese peroxidase
- EC
- 1.11.1.7
- UniProt
- Q02567
- Ligands
- HEM, NAG, CA, MN
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Manganese peroxidase (EC 1.11.1.7) | protein | 357 | 39% helix, 6% strand | Q02567 |
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
- MN · Manganese (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 431 | 0.80 | 0.88 | 44 | MN, HEM |
| 2 | 192 | 0.48 | 0.76 | 32 | empty |
| 3 | 63 | 0.39 | 0.80 | 22 | empty |
Modifications
Observed in the structure: 5 disulfide, 1 glycan (disulfide, N-glycosylation).
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 Q02567
- Elsewhere: RCSB PDB 1MNP · PDBe 1MNP · UniProt Q02567
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