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Crystal structure of the complex of humanized KR127 Fab and PRES1 peptide epitope
Analyse Crystal structure of the complex of humanized KR127 Fab and PRES1 peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EH8
- Type
- protein
- Length
- 446 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Humanized KR127 Fab, light chain; Humanized KR127 Fab, heavy chain; PRES1/PRES2/SURFACE…
- UniProt
- Q2EID8
- Pockets
- 5 · best druggability 0.57
Structure
x-ray diffraction · 3 distinct chains · 7% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Humanized KR127 Fab, light chain | protein | 218 | 6% helix, 50% strand | — |
| H | Humanized KR127 Fab, heavy chain | protein | 218 | 7% helix, 50% strand | — |
| P | PRES1/PRES2/SURFACE protein | protein | 10 | 30% helix, 0% strand | Q2EID8 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 434 | 0.57 | 0.74 | 53 | empty |
| 2 | 114 | 0.39 | 0.75 | 22 | empty |
| 3 | 87 | 0.37 | 0.76 | 18 | empty |
| 4 | 76 | 0.31 | 0.74 | 14 | empty |
| 5 | 55 | 0.29 | 0.75 | 17 | empty |
Interfaces
3 interfaces between chains.
- L–H · 1821 Ų buried · 13 hydrogen bonds · protein-protein
- L–P · 509 Ų buried · 8 hydrogen bonds · protein-protein
- H–P · 311 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2EH8 · Crystal structure of the complex of humanized KR127 fab and PRES1 peptide epitope · the same entry in another collection · chain L against L, 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 Q2EID8
- Elsewhere: RCSB PDB 2EH8 · PDBe 2EH8 · UniProt Q2EID8
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