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The MC179 portion of the cysteine-rich interdomain region (cidr) of a plasmodium falciparum erythrocyte membrane protein-1 (PFEMP1)
Analyse The MC179 portion of the cysteine-rich interdomain region (cidr) of a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C64
- Type
- protein
- Length
- 152 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PFEMP1 variant 2 of strain mc
- UniProt
- Q25734
- Ligands
- CL
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PFEMP1 variant 2 of strain mc | protein | 152 | 76% helix, 0% strand | Q25734 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.41 | 0.75 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3C64 · The MC179 portion of the Cysteine-rich Interdomain Region (CIDR) of a Plasmodium… · 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 Q25734
- Elsewhere: RCSB PDB 3C64 · PDBe 3C64 · UniProt Q25734
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