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Human insulin hexamers with chain B his mutated to tyr

Analyse Human insulin hexamers with chain B his mutated to tyr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QJ0
Type: protein
Length: 100 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Insulin a chain; Insulin B chain
UniProt: P01308
Ligands: ZN, CL

Structure

x-ray diffraction · 3 distinct chains · 57% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Insulin a chain	protein	21	52% helix, 5% strand	P01308
B	Insulin B chain	protein	28	68% helix, 11% strand	P01308
D	Insulin B chain	protein	30	50% helix, 10% strand	P01308

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains B, D
CL · Chloride ion · ion · chains B

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

Interfaces

5 interfaces between chains.

C–D · 800 Å² buried · 7 hydrogen bonds · protein-protein
B–D · 644 Å² buried · 9 hydrogen bonds · protein-protein
A–B · 633 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 61 Å² buried · 1 hydrogen bond · protein-protein
A–D · 31 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1QJ0 · Human insulin hexamers with chain B his mutated to tyr · 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 1QJ0 · PDBe 1QJ0 · UniProt P01308

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