PDBsum entry 1ev6

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protein ligands metals Protein-protein interface(s) links
Hormone/growth factor PDB id
Protein chains
(+ 0 more) 21 a.a.
29 a.a. *
30 a.a. *
CRS ×7
_CL ×2
_ZN ×2
Waters ×240
* Residue conservation analysis
PDB id:
Name: Hormone/growth factor
Title: Structure of the monoclinic form of the m-cresol/insulin r6 hexamer
Structure: Insulin. Chain: a, c, e, g, i, k. Fragment: residues 87-107. Engineered: yes. Insulin. Chain: b, d, f, h, j, l. Fragment: residues 25-54. Engineered: yes
Source: Synthetic: yes. Other_details: this sequence occurs naturally in homo sapiens (human). Sapiens (human)
Biol. unit: Dodecamer (from PQS)
1.90Å     R-factor:   0.195     R-free:   0.235
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
19-Apr-00     Release date:   04-Dec-00    
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Protein chains
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
110 a.a.
21 a.a.
Protein chains
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
110 a.a.
29 a.a.
Protein chain
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
110 a.a.
30 a.a.
Key:    PfamA domain  Secondary structure


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.
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.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19145608 D.Keidel, M.Bonaccio, N.Ghaderi, D.Niks, D.Borchardt, and M.F.Dunn (2009).
1H[19F] NOE NMR structural signatures of the insulin R6 hexamer: evidence of a capped HisB10 site in aryl- and arylacryloyl-carboxylate complexes.
  Chembiochem, 10, 450-453.  
18607693 C.Poulsen, D.Jacobsen, and L.Palm (2008).
Effect of ethylenediamine on chemical degradation of insulin aspart in pharmaceutical solutions.
  Pharm Res, 25, 2534-2544.  
18093308 M.Norrman, and G.Schluckebier (2007).
Crystallographic characterization of two novel crystal forms of human insulin induced by chaotropic agents and a shift in pH.
  BMC Struct Biol, 7, 83.
PDB codes: 2oly 2olz 2om0 2om1
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