Research workbench
Crystal structures of thermotoga maritima CEL5A, apo form and TETRAMER/AU
Analyse Crystal structures of thermotoga maritima CEL5A, apo form and TETRAMER/AU in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AMD
- Type
- protein
- Length
- 1,243 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase
- EC
- 3.2.1.4
- UniProt
- Q9X273
- Pockets
- 10 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Endoglucanase (EC 3.2.1.4) | protein | 311 | 44% helix, 13% strand | Q9X273 |
| B | Endoglucanase (EC 3.2.1.4) | protein | 312 | 42% helix, 13% strand | Q9X273 |
| C | Endoglucanase (EC 3.2.1.4) | protein | 309 | 45% helix, 14% strand | Q9X273 |
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1033 | 0.81 | 0.82 | 96 | empty |
| 2 | 447 | 0.77 | 0.85 | 35 | empty |
| 3 | 638 | 0.74 | 0.81 | 63 | empty |
| 4 | 297 | 0.61 | 0.79 | 33 | empty |
| 5 | 308 | 0.59 | 0.77 | 33 | empty |
Interfaces
6 interfaces between chains.
- A–D · 879 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 647 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 408 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 339 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 146 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3AMD · Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au · 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 Q9X273
- Elsewhere: RCSB PDB 3AMD · PDBe 3AMD · UniProt Q9X273
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