Research workbench
High resolution crystal structure analysis of SERA5 proenzyme from plasmodium falciparum
Analyse High resolution crystal structure analysis of SERA5 proenzyme from plasmodium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6X44
- Type
- protein
- Length
- 773 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine repeat antigen 5
- UniProt
- I0IYW5
- Pockets
- 9 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine repeat antigen 5 | protein | 384 | 37% helix, 17% strand | I0IYW5 |
| B | Serine repeat antigen 5 | protein | 389 | 37% helix, 16% strand | I0IYW5 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.51 | 0.79 | 27 | empty |
| 2 | 170 | 0.48 | 0.77 | 30 | empty |
| 3 | 105 | 0.44 | 0.78 | 34 | empty |
| 4 | 129 | 0.42 | 0.75 | 17 | PEG |
| 5 | 55 | 0.39 | 0.81 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 389 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 6X44 · High Resolution Crystal Structure Analysis of SERA5 proenzyme from plasmodium falciparum · 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 I0IYW5
- Elsewhere: RCSB PDB 6X44 · PDBe 6X44 · UniProt I0IYW5
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