Research workbench
Crystal structure of human bcma in complex with UNIAB(TM) vh
Analyse Crystal structure of human bcma in complex with UNIAB(TM) vh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J7W
- Type
- protein
- Length
- 311 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uniab; Tumor necrosis factor receptor superfamily member 17
- UniProt
- Q02223
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Uniab | protein | 118 | 5% helix, 51% strand | — |
| C | Tumor necrosis factor receptor superfamily member 17 | protein | 39 | 10% helix, 21% strand | Q02223 |
| D | Tumor necrosis factor receptor superfamily member 17 | protein | 36 | 17% helix, 22% strand | Q02223 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 124 | 0.41 | 0.76 | 17 | empty |
| 2 | 57 | 0.26 | 0.73 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–C · 701 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 697 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 249 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 6J7W · Crystal Structure of Human BCMA in complex with UniAb(TM) VH · the same entry in another collection · chain A against A, TM-score 1.00
- Q02223 · AlphaFold monomer V2.0 prediction for tumor necrosis factor receptor superfamily member… · a predicted model of the same protein · chain D against A, TM-score 0.84
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 Q02223
- Elsewhere: RCSB PDB 6J7W · PDBe 6J7W · UniProt Q02223
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