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Crystal structure of destripeptide (B28-B30) insulin

Analyse Crystal structure of destripeptide (B28-B30) insulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HTV
Type: protein
Length: 288 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Insulin
UniProt: P01308
Ligands: ZN
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 54% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, G, I, K	Insulin	protein	21	57% helix, 5% strand	P01308
B, D, F, H, J, L	Insulin	protein	27	52% helix, 11% strand	P01308

Ligands and binding sites

ZN · Zinc ion · metal · chains B, F, J

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	793	0.78	0.82	82	empty
2	92	0.46	0.80	20	empty

Interfaces

31 interfaces between chains.

A–B · 782 Å² buried · 8 hydrogen bonds · protein-protein
I–J · 779 Å² buried · 9 hydrogen bonds · protein-protein
G–H · 761 Å² buried · 8 hydrogen bonds · protein-protein
C–D · 748 Å² buried · 11 hydrogen bonds · protein-protein
E–F · 691 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

1HTV · Crystal structure of destripeptide (B28-B30) insulin · the same entry in another collection · chain A against A, 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 P01308
Elsewhere: RCSB PDB 1HTV · PDBe 1HTV · UniProt P01308

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