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Monoclinic crystalline form of human insulin, complexed with meta- cresol

Analyse Monoclinic crystalline form of human insulin, complexed with meta- cresol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GNQ
Type: protein
Length: 588 residues
Chains: 24
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Insulin
UniProt: P01308
Ligands: CRS, IS8, ZN
Pockets: 7 · best druggability 0.89

Structure

x-ray diffraction · 8 distinct chains · 70% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, G, I, K, M, O, Q, S, U, W	Insulin	protein	21	57% helix, 5% strand	P01308
B, D	Insulin	protein	30	70% helix, 10% strand	P01308
F, T	Insulin	protein	28	71% helix, 11% strand	P01308
H, L	Insulin	protein	29	72% helix, 10% strand	P01308
J	Insulin	protein	28	68% helix, 11% strand	P01308
N, R, X	Insulin	protein	27	74% helix, 11% strand	P01308
P	Insulin	protein	26	73% helix, 12% strand	P01308
V	Insulin	protein	27	70% helix, 11% strand	P01308

Ligands and binding sites

CRS · M-cresol · ligand · 12 copies · chains A, B, F, L, C, D, E, H, G, J, I, K, M, N, R, X, O, P, Q, T, S, V, U, W
IS8 · isothiocyanate · ligand · 4 copies · chains B, J, L, D, F, H, U, N, V, X, P, R, T
ZN · Zinc ion · metal · 4 copies · chains B, J, L, D, F, H, N, V, X, P, R, T
EDO · 1,2-ethanediol · additive · 10 copies · chains A, B, E, D, J, L, F, H, I, P, T, V, Q, R, N, S

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

Pockets

7 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	1081	0.89	0.90	143	IS8, CRS, EDO
2	971	0.84	0.85	107	EDO, CRS
3	494	0.75	0.83	79	ZN, IS8, CRS
4	199	0.64	0.83	32	CRS, EDO
5	174	0.58	0.81	32	CRS

Interfaces

88 interfaces between chains.

B–H · 770 Å² buried · 16 hydrogen bonds · protein-protein
F–L · 745 Å² buried · 16 hydrogen bonds · protein-protein
D–J · 724 Å² buried · 10 hydrogen bonds · protein-protein
N–T · 714 Å² buried · 15 hydrogen bonds · protein-protein
R–X · 668 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 36 disulfide (disulfide).

Compared structures

6GNQ · Monoclinic crystalline form of human insulin, complexed with meta-cresol · 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 6GNQ · PDBe 6GNQ · UniProt P01308

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