Research workbench
Con-ins G1 in complex with the human insulin microreceptor in turn in complex with fv 83-7
Analyse Con-ins G1 in complex with the human insulin microreceptor in turn in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VEQ
- Type
- protein
- Length
- 1,134 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Con-ins G1A a chain; Con-ins G1 B chain; Insulin receptor subunit alpha; Insulin…
- EC
- 2.7.10.1
- UniProt
- A0A0B5AC95, A0A0B5A8Q2, P06213
- Ligands
- NAG, BMA, MAN, FUC, SO4
- Pockets
- 12 · best druggability 0.59
Structure
x-ray diffraction · 9 distinct chains · 10% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, G | Con-ins G1A a chain | protein | 20 | 45% helix, 0% strand | A0A0B5AC95 |
| B, H | Con-ins G1 B chain | protein | 17 | 59% helix, 0% strand | A0A0B5A8Q2 |
| E, K | Insulin receptor subunit alpha (EC 2.7.10.1) | protein | 287 | 10% helix, 30% strand | P06213 |
| F | Insulin receptor (EC 2.7.10.1) | protein | 15 | 53% helix, 0% strand | P06213 |
| C | Fv 83-7 heavy chain | protein | 118 | 3% helix, 50% strand | — |
| D | Fv 83-7 light chain | protein | 114 | 3% helix, 51% strand | — |
| L | Insulin receptor (EC 2.7.10.1) | protein | 11 | 73% helix, 0% strand | P06213 |
| I | Fv 83-7 heavy chain | protein | 117 | 3% helix, 50% strand | — |
| J | Fv 83-7 light chain | protein | 111 | 3% helix, 51% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 14 copies · chains E, C, K, I
- BMA · beta-D-mannopyranose · sugar · 4 copies
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains E, K
- FUC · alpha-L-fucopyranose · sugar · 2 copies · chains E, K
- SO4 · Sulfate ion · ion · 4 copies · chains E, F, D, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 389 | 0.59 | 0.76 | 32 | empty |
| 2 | 196 | 0.48 | 0.76 | 40 | empty |
| 3 | 143 | 0.46 | 0.77 | 27 | FUC |
| 4 | 96 | 0.46 | 0.80 | 24 | NAG |
| 5 | 170 | 0.45 | 0.75 | 21 | empty |
Interfaces
18 interfaces between chains.
- C–D · 899 Ų buried · 11 hydrogen bonds · protein-protein
- I–J · 877 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 587 Ų buried · 4 hydrogen bonds · protein-protein
- H–G · 528 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 520 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 34 disulfide, 10 glycan, 8 modified (disulfide, N-glycosylation, carboxylation, hydroxylation, nonstandard).
Compared structures
- 6VEQ · Con-Ins G1 in complex with the human insulin microreceptor in turn in complex with Fv 83-7 · the same entry in another collection · chain G against G, 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 A0A0B5AC95
- Every structure of UniProt A0A0B5A8Q2
- Every structure of UniProt P06213
- Elsewhere: RCSB PDB 6VEQ · PDBe 6VEQ · UniProt A0A0B5AC95 · UniProt A0A0B5A8Q2 · UniProt P06213
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