UniProt P00725
1,4-beta-D-glucan cellobiohydrolase I (P00725)
1,4-beta-D-glucan cellobiohydrolase I (UniProt P00725), EC 3.2.1.91: 12 experimental structures on GenesisL1, 3 ligands bound, 2 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- P00725
- Protein
- 1,4-beta-D-glucan cellobiohydrolase I
- EC
- 3.2.1.91
- Experimental structures
- 12
- Predicted models
- 0
- Ligands
- 3
- Pockets
- 2 · 2 records with a druggable one
Structures
12 records of P00725 in the MolNFT archive: 12 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1CEL | The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from… | x-ray diffraction | A, B | — | — |
| 1CEL | The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from… | x-ray diffraction | A, B | — | — |
| 1Q2E | Cellobiohydrolase CEL7A with loop deletion 245-252 and bound non-hydrolysable cellotetraose | x-ray diffraction | A, B | — | — |
| 1Q2E | Cellobiohydrolase CEL7A with loop deletion 245-252 and bound non- hydrolysable cellotetraose | x-ray diffraction | A, B | — | — |
| 3CEL | Active-site mutant E212Q determined at pH 6.0 with cellobiose bound in the active site | x-ray diffraction | A | — | — |
| 3CEL | Active-site mutant E212Q determined at pH 6.0 with cellobiose bound in the active site | x-ray diffraction | A | — | — |
| 5CEL | CBH1 (E212Q) cellotetraose complex | x-ray diffraction | A | BGC, NAG, CO | — |
| 5CEL | CBH1 (E212Q) cellotetraose complex | x-ray diffraction | A | — | — |
| 6CEL | CBH1 (E212Q) cellopentaose complex | x-ray diffraction | A | BGC, NAG, CO | 1 (best 0.83) |
| 6CEL | CBH1 (E212Q) cellopentaose complex | x-ray diffraction | A | BGC, NAG, CO | — |
| 7CEL | CBH1 (E217Q) in complex with cellohexaose and cellobiose | x-ray diffraction | A | BGC, NAG, CO | 1 (best 0.83) |
| 7CEL | CBH1 (E217Q) in complex with cellohexaose and cellobiose | x-ray diffraction | A | BGC, NAG, CO | — |
Ligands
Elsewhere
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