Research workbench
Structure of C. elegans htp-2 bound to him-3 closure motif, P21 form
Analyse Structure of C. elegans htp-2 bound to him-3 closure motif, P21 form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4TZL
- Type
- protein
- Length
- 484 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein htp-2; C. elegans him-3 closure motif
- UniProt
- Q95XC8
- Pockets
- 6 · best druggability 0.55
Structure
x-ray diffraction · 4 distinct chains · 31% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein htp-2 | protein | 228 | 33% helix, 27% strand | Q95XC8 |
| B | Protein htp-2 | protein | 226 | 33% helix, 27% strand | Q95XC8 |
| C | C. elegans him-3 closure motif | protein | 14 | 0% helix, 29% strand | — |
| D | C. elegans him-3 closure motif | protein | 16 | 0% helix, 38% strand | — |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.55 | 0.76 | 35 | empty |
| 2 | 66 | 0.42 | 0.81 | 13 | empty |
| 3 | 89 | 0.39 | 0.77 | 24 | empty |
| 4 | 70 | 0.36 | 0.77 | 13 | empty |
| 5 | 52 | 0.35 | 0.79 | 13 | empty |
Interfaces
3 interfaces between chains.
- B–D · 1150 Ų buried · 28 hydrogen bonds · protein-protein
- A–C · 1008 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 360 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4TZL · Structure of C. elegans HTP-2 bound to HIM-3 closure motif, P21 form · 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 Q95XC8
- Elsewhere: RCSB PDB 4TZL · PDBe 4TZL · UniProt Q95XC8
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