Research workbench
0.9 a structure of NP4 from rhodnius prolixus complexed with co at pH 5.6
Analyse 0.9 a structure of NP4 from rhodnius prolixus complexed with co at pH 5.6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YWA
- Type
- protein
- Length
- 184 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitrophorin 4
- UniProt
- Q94734
- Ligands
- HEM, PO4, CMO
- Pockets
- 1 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitrophorin 4 | protein | 184 | 14% helix, 47% strand | Q94734 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A
- CMO · Carbon monoxide · ion · 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 | 314 | 0.77 | 0.87 | 40 | HEM, CMO |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q94734
- Elsewhere: RCSB PDB 1YWA · PDBe 1YWA · UniProt Q94734
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