3P33 | pdb_00003p33

Insulin fibrillation is the Janus face of induced fit. A chiral clamp stabilizes the native state at the expense of activity

Experimental Data Snapshot

  • Method:&nbspX-RAY DIFFRACTION
  • Resolution:&nbsp2.30 Å
  • R-Value Free:&nbsp
    0.299 (Depositor), 0.290 (DCC)&nbsp
  • R-Value Work:&nbsp
    0.214 (Depositor), 0.230 (DCC)&nbsp

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


This is version 1.4 of the entry. See complete&nbsphistory.&nbsp


Literature

Insulin fibrillation is the Janus face of induced fit. A chiral clamp stabilizes the native state at the expense of activity

Hua, Q.X.,&nbspWan, Z.L.,&nbspHuang, K.,&nbspHu, S.Q.,&nbspPhillip, N.F.,&nbspJia, W.H.,&nbspWhittingham, J.,&nbspDodson, G.G.,&nbspKatsoyannis, P.G.,&nbspWeiss, M.A.

To be published.

Macromolecules

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Insulin
A, C, E, G
21Homo sapiensMutation(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, D, F, H
30Homo sapiensMutation(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
Small Molecules
Ligands&nbsp3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
IPH
Query on IPH
Download Ideal Coordinates CCD File&nbsp
I [auth A],
L [auth C],
O [auth E],
R [auth G]		PHENOL
C6 H6 O
ISWSIDIOOBJBQZ-UHFFFAOYSA-N
ZN
Query on ZN
Download Ideal Coordinates CCD File&nbsp
J [auth B],
M [auth D],
P [auth F],
S [auth H]		ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
CL
Query on CL
Download Ideal Coordinates CCD File&nbsp
K [auth B],
N [auth D],
Q [auth F],
T [auth H]		CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
Experimental Data & Validation

Experimental Data

  • Method:&nbspX-RAY DIFFRACTION
  • Resolution:&nbsp2.30 Å
  • R-Value Free:&nbsp 0.299 (Depositor), 0.290 (DCC)&nbsp
  • R-Value Work:&nbsp 0.214 (Depositor), 0.230 (DCC)&nbsp
Space Group:&nbspH 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 77.9α = 90
b = 77.9β = 90
c = 78.3γ = 120
Software Package:
Software NamePurpose
PROTEUM PLUSdata collection
CNSrefinement
PROTEUM PLUSdata reduction
PROTEUM PLUSdata scaling
CNSphasing

Structure Validation

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View more in-depth experimental data
Entry History&nbsp

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-11-23
    Type: Initial release
  • Version 1.1: 2014-10-08
    Changes: Database references
  • Version 1.2: 2014-10-15
    Changes: Derived calculations
  • Version 1.3: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description
  • Version 1.4: 2024-11-20
    Changes: Structure summary