Research workbench
Structure of CFBRCC36-CFKIAA0157 complex (selenium edge)
Analyse Structure of CFBRCC36-CFKIAA0157 complex (selenium edge) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CW4
- Type
- protein
- Length
- 970 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BRCA1/BRCA2-containing complex subunit 3; Protein FAM175B
- UniProt
- E2AXC7, E2AB17
- Ligands
- ZN
- Pockets
- 17 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 45% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BRCA1/BRCA2-containing complex subunit 3 | protein | 247 | 47% helix, 24% strand | E2AXC7 |
| B | Protein FAM175B | protein | 246 | 40% helix, 28% strand | E2AB17 |
| C | BRCA1/BRCA2-containing complex subunit 3 | protein | 233 | 50% helix, 24% strand | E2AXC7 |
| D | Protein FAM175B | protein | 244 | 41% helix, 29% strand | E2AB17 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 684 | 0.77 | 0.82 | 60 | empty |
| 2 | 427 | 0.76 | 0.85 | 36 | empty |
| 3 | 471 | 0.69 | 0.80 | 40 | GOL |
| 4 | 388 | 0.62 | 0.77 | 38 | empty |
| 5 | 316 | 0.62 | 0.79 | 42 | empty |
Interfaces
6 interfaces between chains.
- C–D · 4181 Ų buried · 48 hydrogen bonds · protein-protein
- A–B · 4122 Ų buried · 53 hydrogen bonds · protein-protein
- A–C · 611 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 599 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 584 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 modified (engineered).
Compared structures
- 5CW4 · Structure of CfBRCC36-CfKIAA0157 complex (Selenium Edge) · the same entry in another collection · chain D against D, TM-score 1.00
- E2AB17 · AlphaFold monomer V2.0 prediction for brisc complex subunit FAM175B (E2AB17) · a predicted model of the same protein · chain B against A, TM-score 0.98
- E2AXC7 · AlphaFold monomer V2.0 prediction for lys-63-specific deubiquitinase BRCC36 (E2AXC7) · a predicted model of the same protein · chain C against A, TM-score 0.95
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 E2AXC7
- Every structure of UniProt E2AB17
- Elsewhere: RCSB PDB 5CW4 · PDBe 5CW4 · UniProt E2AXC7 · UniProt E2AB17
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