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Crystalization of human zinc insulin at pH 5.5

Analyse Crystalization of human zinc insulin at pH 5.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CO2
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, CL

Structure

x-ray diffraction · 2 distinct chains · 57% 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	50% helix, 13% strand	P01308

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · 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 · 910 Å² buried · 13 hydrogen bonds · protein-protein
C–D · 904 Å² buried · 12 hydrogen bonds · protein-protein
B–D · 607 Å² buried · 9 hydrogen bonds · protein-protein
B–C · 51 Å² buried · 1 hydrogen bond · protein-protein
A–D · 37 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

5CO2 · Crystalization of human zinc insulin at pH 5.5 · 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 5CO2 · PDBe 5CO2 · UniProt P01308

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