MolNFT v1 · #104509 · protein
PDGF-B blocking antibody bound to PDGF-bb
4QCI · Anti-PDGF-bb antibody - light chain: “PDGF-B blocking antibody bound to PDGF-bb”. X-ray diffraction, 12 pockets (best druggability 0.59). MolNFT v1 #104509 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4QCI
- Type
- protein
- Length
- 1,015 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-PDGF-bb antibody - light chain; Anti-PDGF-bb antibody - heavy chain…
- UniProt
- P01127
- Pockets
- 12 · best druggability 0.59
Structure
x-ray diffraction · 6 distinct chains · 6% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anti-PDGF-bb antibody - light chain | protein | 206 | 8% helix, 51% strand | — |
| B | Anti-PDGF-bb antibody - heavy chain | protein | 214 | 6% helix, 51% strand | — |
| C | Platelet-derived growth factor subunit B | protein | 92 | 4% helix, 61% strand | P01127 |
| D | Platelet-derived growth factor subunit B | protein | 96 | 0% helix, 61% strand | P01127 |
| H | Anti-PDGF-bb antibody - heavy chain | protein | 204 | 6% helix, 52% strand | — |
| L | Anti-PDGF-bb antibody - light chain | protein | 203 | 8% helix, 51% strand | — |
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 487 | 0.59 | 0.74 | 55 | empty |
| 2 | 465 | 0.59 | 0.74 | 51 | empty |
| 3 | 59 | 0.55 | 0.89 | 20 | empty |
| 4 | 105 | 0.51 | 0.82 | 25 | empty |
| 5 | 121 | 0.46 | 0.79 | 19 | empty |
Interfaces
9 interfaces between chains.
- H–L · 1693 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1686 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 1067 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 531 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 518 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 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 P01127
- Elsewhere: RCSB PDB 4QCI · PDBe 4QCI · UniProt P01127
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.