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Crystal structure of the GH5 family catalytic domain of endo-1,4-beta- glucanase CEL5C from butyrivibrio proteoclasticus.
Analyse Crystal structure of the GH5 family catalytic domain of endo-1,4-beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NF7
- Type
- protein
- Length
- 363 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-beta-glucanase CEL5C
- EC
- 3.2.1.4
- UniProt
- E0RXM0
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-glucanase CEL5C (EC 3.2.1.4) | protein | 363 | 39% helix, 12% strand | E0RXM0 |
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 | 346 | 0.58 | 0.76 | 34 | empty |
| 2 | 61 | 0.38 | 0.79 | 16 | empty |
Compared structures
- 4NF7 · Crystal structure of the GH5 family catalytic domain of Endo-1,4-beta-glucanase Cel5C… · 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 E0RXM0
- Elsewhere: RCSB PDB 4NF7 · PDBe 4NF7 · UniProt E0RXM0
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