Research workbench
TBIB1 in complex with the TBIA(ALPHA) leader peptide
Analyse TBIB1 in complex with the TBIA(ALPHA) leader peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5V1V
- Type
- protein
- Length
- 207 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TBIB1; TBIA(ALPHA) leader peptide
- UniProt
- D1CIZ5, D1CIZ1
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 3 distinct chains · 41% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TBIB1 | protein | 88 | 44% helix, 26% strand | D1CIZ5 |
| B | TBIB1 | protein | 85 | 46% helix, 27% strand | D1CIZ5 |
| C, D | TBIA(ALPHA) leader peptide | protein | 17 | 0% helix, 41% strand | D1CIZ1 |
Ligands and binding sites
- ZN · Zinc ion · metal · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 288 | 0.57 | 0.77 | 42 | empty |
| 2 | 127 | 0.46 | 0.78 | 21 | empty |
| 3 | 64 | 0.34 | 0.77 | 14 | empty |
Interfaces
5 interfaces between chains.
- B–D · 1011 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 999 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 312 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 71 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 23 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5V1V · TbiB1 in Complex with the TbiA(alpha) Leader Peptide · 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 D1CIZ5
- Every structure of UniProt D1CIZ1
- Elsewhere: RCSB PDB 5V1V · PDBe 5V1V · UniProt D1CIZ5 · UniProt D1CIZ1
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