MolNFT v1 · #81779 · protein
Compcc in complex with fatty acids
3V2N · Cartilage oligomerization matrix protein (coiled-coil…: “Compcc in complex with fatty acids”. X-ray diffraction, 1 ligand (MYR), 3 pockets (best druggability 0.83). MolNFT v1 #81779 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3V2N
- Type
- protein
- Length
- 225 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cartilage oligomerization matrix protein (coiled-coil domain)
- Ligands
- MYR
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Cartilage oligomerization matrix protein (coiled-coil domain) | protein | 45 | 82% helix, 0% strand | — |
Ligands and binding sites
- MYR · Myristic acid · ligand · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 243 | 0.83 | 0.95 | 34 | MYR |
| 2 | 175 | 0.80 | 0.94 | 26 | empty |
| 3 | 218 | 0.56 | 0.78 | 27 | empty |
Interfaces
10 interfaces between chains.
- D–E · 1193 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 1176 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 1150 Ų buried · 11 hydrogen bonds · protein-protein
- A–E · 1143 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 1119 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 3V2N · COMPcc in complex with fatty acids · 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
- Elsewhere: RCSB PDB 3V2N · PDBe 3V2N
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