MolNFT v1 · #114743 · protein
Crystal structure of engineered trifunctional CTCEL5E
5BYW · Endoglucanase H: “Crystal structure of engineered trifunctional CTCEL5E”. X-ray diffraction, 14 pockets (best druggability 0.88). MolNFT v1 #114743 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5BYW
- Type
- protein
- Length
- 1,596 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase H
- EC
- 3.2.1.4
- UniProt
- P16218
- Pockets
- 14 · best druggability 0.88
Structure
x-ray diffraction · 5 distinct chains · 44% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoglucanase H (EC 3.2.1.4) | protein | 319 | 45% helix, 13% strand | P16218 |
| B | Endoglucanase H (EC 3.2.1.4) | protein | 316 | 45% helix, 13% strand | P16218 |
| C | Endoglucanase H (EC 3.2.1.4) | protein | 318 | 44% helix, 12% strand | P16218 |
| D | Endoglucanase H (EC 3.2.1.4) | protein | 320 | 43% helix, 12% strand | P16218 |
| E | Endoglucanase H (EC 3.2.1.4) | protein | 323 | 43% helix, 12% strand | P16218 |
Pockets
14 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 772 | 0.88 | 0.91 | 76 | empty |
| 2 | 639 | 0.86 | 0.90 | 56 | empty |
| 3 | 492 | 0.83 | 0.90 | 76 | empty |
| 4 | 1002 | 0.77 | 0.79 | 112 | empty |
| 5 | 294 | 0.72 | 0.85 | 54 | empty |
Interfaces
8 interfaces between chains.
- A–D · 1420 Ų buried · 20 hydrogen bonds · protein-protein
- B–E · 1395 Ų buried · 20 hydrogen bonds · protein-protein
- A–E · 484 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 478 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 474 Ų buried · 10 hydrogen bonds · protein-protein
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 P16218
- Elsewhere: RCSB PDB 5BYW · PDBe 5BYW · UniProt P16218
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