Research workbench
Erythromycin esterase erec, mutant H289N in its closed conformation
Analyse Erythromycin esterase erec, mutant H289N in its closed conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XCQ
- Type
- protein
- Length
- 408 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Erec
- UniProt
- C7C425
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erec | protein | 408 | 48% helix, 17% strand | C7C425 |
Ligands and binding sites
- PGO · S-1,2-propanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 751 | 0.82 | 0.85 | 45 | empty |
| 2 | 167 | 0.49 | 0.78 | 26 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6XCQ · Erythromycin esterase EreC, mutant H289N in its closed conformation · 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 C7C425
- Elsewhere: RCSB PDB 6XCQ · PDBe 6XCQ · UniProt C7C425
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