MolNFT v1 · #9811 · protein
Antibody GNC92H2 bound to ligand
1I7Z · Chimera of ig kappa chain: human constant region and mouse…: “Antibody GNC92H2 bound to ligand”. X-ray diffraction, 1 ligand (COC), 11 pockets (best druggability 0.70). MolNFT v1 #9811 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1I7Z
- Type
- protein
- Length
- 878 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chimera of ig kappa chain: human constant region and mouse variable region; Chimera of ig…
- UniProt
- P01834, P01857
- Ligands
- COC
- Pockets
- 11 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Chimera of ig kappa chain: human constant region and mouse variable region | protein | 219 | 6% helix, 50% strand | P01834 |
| B, D | Chimera of ig gamma-1 chain: human constant region and mouse variable region | protein | 220 | 8% helix, 50% strand | P01857 |
Ligands and binding sites
- COC · Cocaine · ligand · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 616 | 0.70 | 0.79 | 65 | empty |
| 2 | 755 | 0.69 | 0.76 | 63 | empty |
| 3 | 158 | 0.68 | 0.87 | 18 | COC |
| 4 | 137 | 0.66 | 0.88 | 19 | COC |
| 5 | 566 | 0.62 | 0.74 | 59 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2083 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 2004 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 900 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 485 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 22 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 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 P01834
- Every structure of UniProt P01857
- Elsewhere: RCSB PDB 1I7Z · PDBe 1I7Z · UniProt P01834 · UniProt P01857
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