MolNFT v1 · #55376 · protein
Catalytic domain of clostridium thermocellum celt
2YIK · Endoglucanase: “Catalytic domain of clostridium thermocellum celt”. X-ray diffraction, 2 ligands (CA, ZN), 2 pockets (best druggability 0.51). MolNFT v1 #55376 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2YIK
- Type
- protein
- Length
- 493 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase
- EC
- 3.2.1.4
- UniProt
- Q8VV73
- Ligands
- CA, ZN
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoglucanase (EC 3.2.1.4) | protein | 493 | 47% helix, 8% strand | Q8VV73 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 199 | 0.51 | 0.77 | 25 | empty |
| 2 | 70 | 0.45 | 0.82 | 15 | empty |
Compared structures
- 2YIK · Catalytic domain of Clostridium thermocellum CelT · 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 Q8VV73
- Elsewhere: RCSB PDB 2YIK · PDBe 2YIK · UniProt Q8VV73
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