Research workbench
Structure of C. elegans htp-1 bound to him-3 closure motif
Analyse Structure of C. elegans htp-1 bound to him-3 closure motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4TZO
- Type
- protein
- Length
- 1,000 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein htp-1; C. elegans him-3 closure motif
- UniProt
- Q20305, G5EBG0
- Pockets
- 12 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | Protein htp-1 | protein | 236 | 32% helix, 28% strand | Q20305 |
| B, D, F, H | C. elegans him-3 closure motif | protein | 14 | 0% helix, 43% strand | G5EBG0 |
Pockets
12 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.55 | 0.79 | 28 | empty |
| 2 | 128 | 0.50 | 0.80 | 24 | empty |
| 3 | 109 | 0.48 | 0.80 | 23 | empty |
| 4 | 230 | 0.47 | 0.74 | 30 | empty |
| 5 | 73 | 0.43 | 0.81 | 19 | empty |
Interfaces
12 interfaces between chains.
- G–H · 1108 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1101 Ų buried · 23 hydrogen bonds · protein-protein
- E–F · 1069 Ų buried · 23 hydrogen bonds · protein-protein
- C–D · 1067 Ų buried · 21 hydrogen bonds · protein-protein
- A–G · 324 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 4TZO · Structure of C. elegans HTP-1 bound to HIM-3 closure motif · 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 Q20305
- Every structure of UniProt G5EBG0
- Elsewhere: RCSB PDB 4TZO · PDBe 4TZO · UniProt Q20305 · UniProt G5EBG0
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