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Crystal structure of form B monoclinic crystal of insulin

Analyse Crystal structure of form B monoclinic crystal of insulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WAV
Type
protein
Length
306 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Insulin
UniProt
P01315
Ligands
IPH, ZN
Pockets
8 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 61% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, G, I, KInsulinprotein2148% helix, 0% strandP01315
B, D, F, H, J, LInsulinprotein3070% helix, 10% strandP01315

Ligands and binding sites

  • IPH · Phenol · ligand · 6 copies · chains A, B, F, C, D, L, E, J, G, H, K, I
  • ZN · Zinc ion · metal · 2 copies · chains B, F, J, D, H, L

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

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14280.820.9063IPH
22010.660.8430IPH
31820.650.8532IPH
41320.610.8526IPH
51420.610.8430IPH

Interfaces

37 interfaces between chains.

  • F–H · 702 Ų buried · 8 hydrogen bonds · protein-protein
  • A–B · 679 Ų buried · 6 hydrogen bonds · protein-protein
  • J–L · 676 Ų buried · 9 hydrogen bonds · protein-protein
  • C–D · 653 Ų buried · 2 hydrogen bonds · protein-protein
  • B–D · 646 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

  • 1WAV · Crystal structure of form B monoclinic crystal of insulin · the same entry in another collection · chain A against A, TM-score 1.00

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