3JSD | pdb_00003jsd

Insulin's biosynthesis and activity have opposing structural requirements: a new factor in neonatal diabetes mellitus


Experimental Data Snapshot

  • Method:&nbspX-RAY DIFFRACTION
  • Resolution:&nbsp2.50 Å
  • R-Value Free:&nbsp
    0.274 (Depositor)&nbsp
  • R-Value Work:&nbsp
    0.206 (Depositor), 0.230 (DCC)&nbsp
  • R-Value Observed:&nbsp
    0.206&nbsp(Depositor)&nbsp

Starting Model: experimental
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wwPDB Validation&nbsp &nbsp3D Report&nbspFull Report


This is version 1.5 of the entry. See complete&nbsphistory.&nbsp


Literature

Insulin's biosynthesis and activity have opposing structural requirements: a new factor in neonatal diabetes mellitus

Weiss, M.A.,&nbspWan, Z.L.,&nbspDodson, E.J.,&nbspLiu, M.,&nbspXu, B.,&nbspHua, Q.X.,&nbspTurkenburg, M.,&nbspWhittingham, J.,&nbspNakagawa, S.H.,&nbspHuang, K.,&nbspHu, S.Q.,&nbspJia, W.H.,&nbspWang, S.H.,&nbspBrange, J.,&nbspWhittaker, J.,&nbspArvan, P.,&nbspKatsoyannis, P.G.,&nbspDodson, G.G.

To be published.

Macromolecules

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Insulin A chain
A, C
21N/AMutation(s): 0&nbsp
UniProt & NIH Common Fund Data Resources
Find proteins for&nbspP01308&nbsp(Homo sapiens)
Explore&nbspP01308&nbsp
Go to UniProtKB: &nbspP01308
PHAROS: &nbspP01308
GTEx: &nbspENSG00000254647&nbsp
Entity Groups &nbsp
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01308
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Insulin B chain
B, D
30N/AMutation(s): 1&nbsp
UniProt & NIH Common Fund Data Resources
Find proteins for&nbspP01308&nbsp(Homo sapiens)
Explore&nbspP01308&nbsp
Go to UniProtKB: &nbspP01308
PHAROS: &nbspP01308
GTEx: &nbspENSG00000254647&nbsp
Entity Groups &nbsp
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01308
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method:&nbspX-RAY DIFFRACTION
  • Resolution:&nbsp2.50 Å
  • R-Value Free:&nbsp 0.274 (Depositor)&nbsp
  • R-Value Work:&nbsp 0.206 (Depositor), 0.230 (DCC)&nbsp
  • R-Value Observed:&nbsp0.206&nbsp(Depositor)&nbsp
Space Group:&nbspH 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 80.843α = 90
b = 80.843β = 90
c = 38.842γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
CNSrefinement
SCALEPACKdata scaling
CNSphasing

Structure Validation

View&nbspFull Validation Report



Entry History&nbsp

Revision History  (Full details and data files)

  • Version 1.0: 2010-09-15
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2017-11-01
    Changes: Refinement description
  • Version 1.3: 2021-10-13
    Changes: Database references, Derived calculations
  • Version 1.4: 2023-09-06
    Changes: Data collection, Refinement description
  • Version 1.5: 2024-10-30
    Changes: Structure summary