Research workbench
ENDO/EXOCELLULASE from thermomonospora
Analyse ENDO/EXOCELLULASE from thermomonospora in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TF4
- Type
- protein
- Length
- 1,210 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T. fusca ENDO/EXO-cellulase E4 catalytic domain and cellulose-binding domain
- EC
- 3.2.1.4
- UniProt
- P26221
- Ligands
- CA
- Pockets
- 6 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | T. fusca ENDO/EXO-cellulase E4 catalytic domain and cellulose-binding domain (EC 3.2.1.4) | protein | 605 | 38% helix, 15% strand | P26221 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 321 | 0.58 | 0.77 | 37 | empty |
| 2 | 299 | 0.56 | 0.76 | 37 | empty |
| 3 | 118 | 0.36 | 0.73 | 22 | empty |
| 4 | 82 | 0.33 | 0.74 | 16 | empty |
| 5 | 80 | 0.32 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 288 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 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 P26221
- Elsewhere: RCSB PDB 1TF4 · PDBe 1TF4 · UniProt P26221
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