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Crystal structure of KTI13/ATS1
Analyse Crystal structure of KTI13/ATS1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4D4Q
- Type
- protein
- Length
- 648 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein ATS1
- UniProt
- P31386
- Pockets
- 9 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein ATS1 | protein | 329 | 1% helix, 48% strand | P31386 |
| B | Protein ATS1 | protein | 319 | 1% helix, 47% strand | P31386 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 527 | 0.75 | 0.83 | 46 | empty |
| 2 | 569 | 0.75 | 0.82 | 49 | empty |
| 3 | 121 | 0.55 | 0.83 | 29 | empty |
| 4 | 266 | 0.55 | 0.76 | 23 | empty |
| 5 | 89 | 0.50 | 0.83 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 580 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
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 P31386
- Elsewhere: RCSB PDB 4D4Q · PDBe 4D4Q · UniProt P31386
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