MolNFT v1 · #11089 · protein

Non-standard design of unstable insulin analogues with enhanced activity

1JCA: “Non-standard design of unstable insulin analogues with enhanced activity”. X-ray diffraction, 1 ligand (ZN). MolNFT v1 #11089 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1JCA
Type: protein
Length: 101 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Insulin a; Insulin B
UniProt: P01308
Ligands: ZN

Structure

x-ray diffraction · 3 distinct chains · 56% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Insulin a	protein	21	52% helix, 5% strand	P01308
B	Insulin B	protein	30	50% helix, 10% strand	P01308
D	Insulin B	protein	29	66% helix, 10% strand	P01308

Ligands and binding sites

ZN · Zinc 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.

A–B · 788 Å² buried · 8 hydrogen bonds · protein-protein
B–D · 706 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 635 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 60 Å² buried · 1 hydrogen bond · protein-protein
B–C · 30 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1JCA · Non-standard Design of Unstable Insulin Analogues with Enhanced Activity · 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 1JCA · PDBe 1JCA · UniProt P01308

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