Research workbench
Crystal structure of eba-175 region II (rii)
Analyse Crystal structure of eba-175 region II (rii) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZRL
- Type
- protein
- Length
- 583 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Erythrocyte binding antigen region II
- UniProt
- Q25735
- Ligands
- SO4, CL
- Pockets
- 9 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erythrocyte binding antigen region II | protein | 583 | 62% helix, 3% strand | Q25735 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 650 | 0.73 | 0.80 | 66 | SO4 |
| 2 | 115 | 0.61 | 0.86 | 24 | empty |
| 3 | 295 | 0.58 | 0.77 | 37 | empty |
| 4 | 119 | 0.46 | 0.78 | 29 | empty |
| 5 | 110 | 0.44 | 0.78 | 19 | SO4 |
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 1ZRL · Crystal structure of EBA-175 Region II (RII) · 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 Q25735
- Elsewhere: RCSB PDB 1ZRL · PDBe 1ZRL · UniProt Q25735
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