PDBsum entry 1ev3

Hormone/growth factor

PDB id: 1ev3

Contents

Protein chains

21 a.a.

28 a.a. *

Ligands

CRS ×3

Metals

_CL ×2

_ZN ×2

Waters ×90

* Residue conservation analysis

PDB id:

1ev3

Name:

Hormone/growth factor

Title:

Structure of the rhombohedral form of the m-cresol/insulin r6 hexamer

Structure:

Insulin. Chain: a, c. Fragment: residues 87-107. Engineered: yes. Insulin. Chain: b, d. Fragment: residues 25-54. Engineered: yes

Source:

Synthetic: yes. Other_details: this sequence occurs naturally in homo sapiens (human). (Human)

Biol. unit:

Dodecamer (from PDB file)

Resolution:

1.78Å R-factor: 0.200 R-free: 0.266

Authors:

G.D.Smith,E.Ciszak,L.A.Magrum,W.A.Pangborn,R.H.Blessing

Key ref:

G.D.Smith et al. (2000). R6 hexameric insulin complexed with m-cresol or resorcinol. Acta Crystallogr D Biol Crystallogr, 56, 1541-1548. PubMed id: 11092919 DOI: 10.1107/S0907444900012749

Date:

19-Apr-00 Release date: 04-Dec-00

Protein chains

P01308  (INS_HUMAN) -  Insulin from Homo sapiens

Seq: 110 a.a.

Struc: 21 a.a.

Protein chains

P01308  (INS_HUMAN) -  Insulin from Homo sapiens

Seq: 110 a.a.

Struc: 28 a.a.

DOI no: 10.1107/S0907444900012749

Acta Crystallogr D Biol Crystallogr 56:1541-1548 (2000)

PubMed id: 11092919

R6 hexameric insulin complexed with m-cresol or resorcinol.

G.D.Smith, E.Ciszak, L.A.Magrum, W.A.Pangborn, R.H.Blessing.

ABSTRACT

The structures of three R(6) human insulin hexamers have been determined. Crystals of monoclinic m-cresol-insulin, monoclinic resorcinol-insulin and rhombohedral m-cresol-insulin diffracted to 1. 9, 1.9 and 1.78 A, respectively, and have been refined to residuals of 0.195, 0.179 and 0.200, respectively. In all three structures, a phenolic derivative is found to occupy the phenolic binding site, where it forms hydrogen bonds to the carbonyl O atom of CysA6 and the N atom of CysA11. Two additional phenolic derivative binding sites were identified within or between hexamers. The structures of all three hexamers are nearly identical, although a large displacement of the N-terminus of one B chain in both monoclinic structures results from coordination to a sodium ion which is located between symmetry-related hexamers. Other minor differences in structure arise from differences in packing in the monoclinic cell compared with the rhombohedral cell. Based upon the differences in conformation of the GluB13 side chains in T(6), T(3)R(f)(3) and R(6) hexamers, the deprotonation of these side chains appears to be associated with the T-->R conformational transition.

Selected figure(s)

Figure 3.
Figure 3 SETOR drawing (Evans, 1993[Evans, S. V. (1993). J. Mol. Graph. 6, 244-245.]) of B chain Glu13 residues in (a) T[6] human insulin, (b) T[3]R human insulin, (c) monoclinic m-cresol human insulin, (d) monoclinic resorcinol human insulin and (e) rhombohedral m-cresol human insulin.

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2000, 56, 1541-1548) copyright 2000.

Figure was selected by an automated process.