MolNFT v1 · #53358 · protein

Semi-synthetic analogue of human insulin PROB26-dti

2WS7 · Insulin a chain: “Semi-synthetic analogue of human insulin PROB26-dti”. X-ray diffraction, 3 ligands (IPH, ZN, CL), 8 pockets (best druggability 0.86). MolNFT v1 #53358 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2WS7
Type: protein
Length: 252 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Insulin a chain; Insulin B chain
UniProt: P01308
Ligands: IPH, ZN, CL
Pockets: 8 · best druggability 0.86

Structure

x-ray diffraction · 10 distinct chains · 70% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Insulin a chain	protein	20	50% helix, 0% strand	P01308
B	Insulin B chain	protein	19	84% helix, 0% strand	P01308
C, G, I	Insulin a chain	protein	21	48% helix, 0% strand	P01308
D	Insulin B chain	protein	23	74% helix, 0% strand	P01308
E	Insulin a chain	protein	20	55% helix, 0% strand	P01308
F	Insulin B chain	protein	20	80% helix, 0% strand	P01308
H	Insulin B chain	protein	26	77% helix, 0% strand	P01308
J	Insulin B chain	protein	21	81% helix, 0% strand	P01308
K	Insulin a chain	protein	19	68% helix, 0% strand	P01308
L	Insulin B chain	protein	21	81% helix, 0% strand	P01308

Ligands and binding sites

IPH · Phenol · ligand · 6 copies · chains A, B, F, H, C, D, J, L, E, G, I, K
ZN · Zinc ion · metal · 2 copies · chains B, F, J, D, H, L
CL · Chloride ion · ion · 2 copies · chains B, F, J, D, H, L

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

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	505	0.86	0.92	66	IPH
2	107	0.69	0.91	24	IPH
3	76	0.64	0.91	22	IPH
4	69	0.63	0.91	22	IPH
5	277	0.53	0.75	27	empty

Interfaces

37 interfaces between chains.

G–H · 477 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 420 Å² buried · 0 hydrogen bonds · protein-protein
B–D · 403 Å² buried · 8 hydrogen bonds · protein-protein
F–H · 399 Å² buried · 3 hydrogen bonds · protein-protein
K–L · 396 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

2WS7 · Semi-synthetic analogue of human insulin ProB26-DTI · 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 2WS7 · PDBe 2WS7 · UniProt P01308

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