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Structure of porcine insulin cocrystallized with clupeine Z

Analyse Structure of porcine insulin cocrystallized with clupeine Z in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7INS
Type
protein
Length
169 residues
Chains
7
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Insulin (chain a); Insulin (chain B); General protamine chain
UniProt
P01315
Ligands
CRS, UNK, ZN
Pockets
3 · best druggability 0.51

Structure

x-ray diffraction · 3 distinct chains · 51% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, EInsulin (chain a)protein2162% helix, 5% strandP01315
B, D, FInsulin (chain B)protein3070% helix, 3% strandP01315
GGeneral protamine chainprotein160% helix, 0% strand—

Ligands and binding sites

  • CRS · M-cresol · ligand · 3 copies · chains A, B, D, G, C, F, E
  • UNK · Unknown · ligand · 2 copies · chains D, F, C, G
  • ZN · Zinc ion · metal · chains B, D, F, G

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1810.510.8315CRS, UNK
2740.500.8415CRS
3940.500.8223CRS

Interfaces

15 interfaces between chains.

  • B–G · 699 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 607 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 605 Ų buried · 5 hydrogen bonds · protein-protein
  • E–F · 605 Ų buried · 2 hydrogen bonds · protein-protein
  • D–G · 525 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

  • 7INS · Structure of porcine insulin cocrystallized with clupeine Z · the same entry in another collection · chain A against A, TM-score 1.00

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