Research workbench
Human CD38 in complex with nanobody MU551
Analyse Human CD38 in complex with nanobody MU551 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5F1O
- Type
- protein
- Length
- 369 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosyl CYCLASE/CYCLIC ADP-ribose hydrolase 1; Nanobody MU551
- EC
- 3.2.2.6
- UniProt
- P28907
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosyl CYCLASE/CYCLIC ADP-ribose hydrolase 1 (EC 3.2.2.6) | protein | 241 | 43% helix, 14% strand | P28907 |
| B | Nanobody MU551 | protein | 128 | 13% helix, 51% strand | — |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 304 | 0.56 | 0.76 | 36 | empty |
| 2 | 95 | 0.55 | 0.84 | 15 | empty |
| 3 | 95 | 0.35 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 950 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
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 P28907
- Elsewhere: RCSB PDB 5F1O · PDBe 5F1O · UniProt P28907
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