Research workbench
Complex of anti-human il-2 antibody and human il-2
Analyse Complex of anti-human il-2 antibody and human il-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DR4
- Type
- protein
- Length
- 2,174 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-human il-2 antibody, mouse ig G, heavy chain; Anti-human il-2 antibody, mouse ig G…
- UniProt
- P60568
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 12 distinct chains · 19% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | Anti-human il-2 antibody, mouse ig G, heavy chain | protein | 221 | 4% helix, 53% strand | — |
| L | Anti-human il-2 antibody, mouse ig G, kappa chain | protein | 212 | 6% helix, 53% strand | — |
| A | Anti-human il-2 antibody, mouse ig G, heavy chain | protein | 212 | 6% helix, 53% strand | — |
| B | Anti-human il-2 antibody, mouse ig G, kappa chain | protein | 179 | 4% helix, 46% strand | — |
| C | Anti-human il-2 antibody, mouse ig G, heavy chain | protein | 218 | 7% helix, 52% strand | — |
| D | Anti-human il-2 antibody, mouse ig G, kappa chain | protein | 213 | 7% helix, 54% strand | — |
| E | Anti-human il-2 antibody, mouse ig G, heavy chain | protein | 216 | 6% helix, 52% strand | — |
| F | Anti-human il-2 antibody, mouse ig G, kappa chain | protein | 211 | 6% helix, 56% strand | — |
| G | Interleukin-2 | protein | 123 | 64% helix, 8% strand | P60568 |
| I | Interleukin-2 | protein | 122 | 66% helix, 10% strand | P60568 |
| J | Interleukin-2 | protein | 125 | 67% helix, 3% strand | P60568 |
| K | Interleukin-2 | protein | 122 | 66% helix, 8% strand | P60568 |
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 696 | 0.75 | 0.81 | 90 | empty |
| 2 | 678 | 0.72 | 0.79 | 62 | empty |
| 3 | 500 | 0.72 | 0.81 | 55 | empty |
| 4 | 291 | 0.63 | 0.80 | 41 | empty |
| 5 | 450 | 0.62 | 0.77 | 56 | empty |
Interfaces
25 interfaces between chains.
- H–L · 1784 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1771 Ų buried · 14 hydrogen bonds · protein-protein
- E–F · 1701 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1620 Ų buried · 14 hydrogen bonds · protein-protein
- G–I · 585 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 19 disulfide (disulfide).
Compared structures
- 7DR4 · Complex of anti-human IL-2 antibody and human IL-2 · the same entry in another collection · chain K against K, 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
- Every structure of UniProt P60568
- Elsewhere: RCSB PDB 7DR4 · PDBe 7DR4 · UniProt P60568
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