MolNFT v1 · #1454 · protein

PH affects glu B13 switching and sulfate binding in cubic insulin crystals (pH 6.50 coordinates)

1B2E · Protein (insulin a chain): “PH affects glu B13 switching and sulfate binding in cubic insulin crystals (pH 6.50 coordinates)”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #1454 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1B2E
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 · 53% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (insulin a chain)	protein	21	62% 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 · 797 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1B2E · PH affects glu B13 switching and sulfate binding in cubic insulin crystals (pH 6.50… · 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 0.37

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 1B2E · PDBe 1B2E · UniProt P01315

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