Research workbench
SCCTS1_KINETIN crystal structure
Analyse SCCTS1_KINETIN crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2UY5
- Type
- protein
- Length
- 285 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endochitinase
- EC
- 3.2.1.14
- UniProt
- P29029
- Ligands
- H35
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endochitinase (EC 3.2.1.14) | protein | 285 | 33% helix, 20% strand | P29029 |
Ligands and binding sites
- H35 · N-(furan-2-ylmethyl)-7H-purin-6-amine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.45 | 0.80 | 31 | H35 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 P29029
- Elsewhere: RCSB PDB 2UY5 · PDBe 2UY5 · UniProt P29029
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