MolNFT v1 · #26650 · protein
Structure of chemically modified myoglobin with distal N- tetrazolyl-histidine E7(64)
1WVP: “Structure of chemically modified myoglobin with distal N- tetrazolyl-histidine E7(64)”. X-ray diffraction, 2 ligands (HEM, SO4), 1 pocket (best druggability 0.67). MolNFT v1 #26650 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1WVP
- Type
- protein
- Length
- 151 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myoglobin
- UniProt
- P02185
- Ligands
- HEM, SO4
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myoglobin | protein | 151 | 78% helix, 0% strand | P02185 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- SO4 · Sulfate ion · ion · 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 | 151 | 0.67 | 0.87 | 26 | HEM |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 1WVP · Structure of chemically modified myoglobin with distal N-tetrazolyl-histidine E7(64) · the same entry in another collection · 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 P02185
- Elsewhere: RCSB PDB 1WVP · PDBe 1WVP · UniProt P02185
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