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Crystal structures of thermotoga maritima CEL5A, apo form and DIMER/AU
Analyse Crystal structures of thermotoga maritima CEL5A, apo form and DIMER/AU in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AMC
- Type
- protein
- Length
- 614 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase
- EC
- 3.2.1.4
- UniProt
- Q9X273
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoglucanase (EC 3.2.1.4) | protein | 308 | 44% helix, 13% strand | Q9X273 |
| B | Endoglucanase (EC 3.2.1.4) | protein | 306 | 44% helix, 14% strand | Q9X273 |
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 | 1084 | 0.81 | 0.82 | 102 | empty |
| 2 | 115 | 0.48 | 0.79 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 819 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3AMC · Crystal structures of Thermotoga maritima Cel5A, apo form and dimer/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 3AMC · PDBe 3AMC · UniProt Q9X273
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