MolNFT v1 · #140920 · protein
Crystal structure of the pH-like domain of LAM6
5YQR · ENDOLYSIN/MEMBRANE-anchored lipid-binding protein LAM6…: “Crystal structure of the pH-like domain of LAM6”. X-ray diffraction, 1 pocket (best druggability 0.52). MolNFT v1 #140920 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5YQR
- Type
- protein
- Length
- 268 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ENDOLYSIN/MEMBRANE-anchored lipid-binding protein LAM6 fusion protein
- EC
- 3.2.1.17
- UniProt
- P00720, Q08001
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ENDOLYSIN/MEMBRANE-anchored lipid-binding protein LAM6 fusion protein (EC 3.2.1.17) | protein | 268 | 48% helix, 20% strand | P00720, Q08001 |
Ligands and binding sites
- 2PE · Nonaethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 235 | 0.52 | 0.76 | 30 | empty |
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 P00720
- Every structure of UniProt Q08001
- Elsewhere: RCSB PDB 5YQR · PDBe 5YQR · UniProt P00720 · UniProt Q08001
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