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Radiation damage study of cu T6-insulin - 0.30 mgy

Analyse Radiation damage study of cu T6-insulin - 0.30 mgy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4M4J
Type: protein
Length: 100 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Insulin
UniProt: P01317
Ligands: CU

Structure

x-ray diffraction · 3 distinct chains · 53% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Insulin	protein	21	67% helix, 10% strand	P01317
B	Insulin	protein	28	50% helix, 14% strand	P01317
D	Insulin	protein	30	47% helix, 13% strand	P01317

Ligands and binding sites

CU · Copper (II) ion · metal · 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.

C–D · 898 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 838 Å² buried · 14 hydrogen bonds · protein-protein
B–D · 626 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 62 Å² buried · 1 hydrogen bond · protein-protein
A–D · 48 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

4M4J · Radiation damage study of Cu T6-insulin - 0.30 MGy · 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 P01317
Elsewhere: RCSB PDB 4M4J · PDBe 4M4J · UniProt P01317

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