Research workbench
Human FLRT3 lrr domain
Analyse Human FLRT3 lrr domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CMP
- Type
- protein
- Length
- 1,290 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leucine-rich repeat transmembrane protein FLRT3
- UniProt
- Q9NZU0
- Ligands
- NAG
- Pockets
- 16 · best druggability 0.74
Structure
x-ray diffraction · 4 distinct chains · 10% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leucine-rich repeat transmembrane protein FLRT3 | protein | 324 | 11% helix, 17% strand | Q9NZU0 |
| B | Leucine-rich repeat transmembrane protein FLRT3 | protein | 323 | 11% helix, 18% strand | Q9NZU0 |
| C | Leucine-rich repeat transmembrane protein FLRT3 | protein | 322 | 9% helix, 18% strand | Q9NZU0 |
| D | Leucine-rich repeat transmembrane protein FLRT3 | protein | 321 | 10% helix, 17% strand | Q9NZU0 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1119 | 0.74 | 0.77 | 79 | empty |
| 2 | 155 | 0.62 | 0.85 | 22 | empty |
| 3 | 479 | 0.62 | 0.75 | 37 | empty |
| 4 | 382 | 0.61 | 0.77 | 44 | empty |
| 5 | 442 | 0.60 | 0.75 | 32 | empty |
Interfaces
4 interfaces between chains.
- A–D · 1259 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 402 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 364 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 243 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide, 4 glycan (disulfide, N-glycosylation).
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 Q9NZU0
- Elsewhere: RCSB PDB 5CMP · PDBe 5CMP · UniProt Q9NZU0
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