Research workbench
X-ray crystal structure of the catalytic domain of thermobifida fusca endoglucanase CEL5A (E5) E355Q in complex with cellotetraose
Analyse X-ray crystal structure of the catalytic domain of thermobifida fusca… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CKR
- Type
- protein
- Length
- 610 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase E-5
- EC
- 3.2.1.4
- UniProt
- Q01786
- Ligands
- BEN, BGC, ZN, NA
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Endoglucanase E-5 (EC 3.2.1.4) | protein | 305 | 44% helix, 17% strand | Q01786 |
Ligands and binding sites
- BEN · Benzamidine · ligand · 2 copies · chains A, B
- BGC · beta-D-glucopyranose · sugar · 5 copies · chains B
- ZN · Zinc ion · metal · 5 copies · chains A, B
- NA · Sodium ion · metal · chains B
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 367 | 0.57 | 0.75 | 60 | PG4 |
| 2 | 141 | 0.49 | 0.79 | 26 | BGC |
| 3 | 98 | 0.38 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 143 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2CKR · X-ray crystal structure of the catalytic domain of thermobifida fusca endoglucanase CEL5A… · 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 Q01786
- Elsewhere: RCSB PDB 2CKR · PDBe 2CKR · UniProt Q01786
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