MolNFT v1 · #109754 · protein

Insulin co-crystallizes in the presence of it beta-cell chaperone sulfatide

4XC4: “Insulin co-crystallizes in the presence of it beta-cell chaperone sulfatide”. X-ray diffraction, 3 ligands (ZN, NA, CL). MolNFT v1 #109754 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4XC4
Type: protein
Length: 102 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Insulin
UniProt: P01308
Ligands: ZN, NA, CL

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Insulin	protein	21	67% helix, 10% strand	P01308
B, D	Insulin	protein	30	47% helix, 13% strand	P01308

Ligands and binding sites

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

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

Interfaces

5 interfaces between chains.

A–B · 892 Å² buried · 10 hydrogen bonds · protein-protein
C–D · 880 Å² buried · 11 hydrogen bonds · protein-protein
B–D · 626 Å² buried · 8 hydrogen bonds · protein-protein
A–D · 59 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 49 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

4XC4 · Insulin co-crystallizes in the presence of it beta-cell chaperone sulfatide · 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 4XC4 · PDBe 4XC4 · UniProt P01308

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