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PH affects glu B13 switching and sulfate binding in cubic insulin crystals (pH 5.00 coordinates)

Analyse PH affects glu B13 switching and sulfate binding in cubic insulin crystals (pH… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1B17
Type: protein
Length: 51 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (insulin a chain); Protein (insulin B chain)
UniProt: P01315
Ligands: SO4

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (insulin a chain)	protein	21	67% helix, 5% strand	P01315
B	Protein (insulin B chain)	protein	30	47% helix, 3% strand	P01315

Ligands and binding sites

SO4 · Sulfate ion · ion · chains B

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

Interfaces

1 interface between chains.

A–B · 776 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1B17 · PH affects glu B13 switching and sulfate binding in cubic insulin crystals (pH 5.00… · the same entry in another collection · chain A against A, TM-score 1.00
P01315 · AlphaFold monomer V2.0 prediction for insulin (P01315) · a predicted model of the same protein · chain B against A, TM-score 0.38

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 P01315
Elsewhere: RCSB PDB 1B17 · PDBe 1B17 · UniProt P01315

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