MolNFT v1 · #107814 · protein
Mcg - a dimer of lambda variable domains
4UNU · Ig lambda chain V-II region mgc: “Mcg - a dimer of lambda variable domains”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.50). MolNFT v1 #107814 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4UNU
- Type
- protein
- Length
- 218 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ig lambda chain V-II region mgc
- UniProt
- P01709
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ig lambda chain V-II region mgc | protein | 109 | 3% helix, 49% strand | P01709 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains B, A
- 15P · Polyethylene glycol (N=34) · 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 | 119 | 0.50 | 0.81 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 549 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 P01709
- Elsewhere: RCSB PDB 4UNU · PDBe 4UNU · UniProt P01709
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