Research workbench
The enterococcus faecalis mscramm ACE binds its ligands by the collagen hug model
Analyse The enterococcus faecalis mscramm ACE binds its ligands by the collagen hug… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z1P
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen adhesin protein
- UniProt
- Q836L2
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Collagen adhesin protein | protein | 282 | 4% helix, 48% strand | Q836L2 |
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 | 103 | 0.59 | 0.87 | 24 | empty |
| 2 | 75 | 0.33 | 0.75 | 15 | empty |
Compared structures
- 2Z1P · The Enterococcus faecalis MSCRAMM ACE binds its ligands by the collagen Hug Model · 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 Q836L2
- Elsewhere: RCSB PDB 2Z1P · PDBe 2Z1P · UniProt Q836L2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.