Download MendeleyInsulin with proline analog ThioP at position B28 in the T2 state
Lieblich, S.A., Fang, K.Y., Tirrell, D.A.To be published.
5UU2
Insulin with proline analog ThioP at position B28 in the T2 state
- PDB DOI: https://doi.org/10.2210/pdb5UU2/pdb
- Classification: HORMONE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2017-02-15 Released: 2018-02-21
- Funding Organization(s): Novo Nordisk Foundation
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.22 Å
- R-Value Free: 0.156
- R-Value Work: 0.138
- R-Value Observed: 0.139
wwPDB Validation 3D Report Full Report
This is version 1.2 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by: Sequence | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Insulin Chain A | 21 | Homo sapiens | Mutation(s): 0 Gene Names: INS |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P01308 (Homo sapiens) Explore P01308 Go to UniProtKB: P01308 | |||||
PHAROS: P01308 GTEx: ENSG00000254647 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P01308 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Insulin Chain B | 30 | Homo sapiens | Mutation(s): 0 Gene Names: INS |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P01308 (Homo sapiens) Explore P01308 Go to UniProtKB: P01308 | |||||
PHAROS: P01308 GTEx: ENSG00000254647 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P01308 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| PRS Query on PRS | B | L-PEPTIDE LINKING | C4 H7 N O2 S |  | PRO |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.22 Å
- R-Value Free: 0.156
- R-Value Work: 0.138
- R-Value Observed: 0.139
- Space Group: I 21 3
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 78.067 | α = 90 |
| b = 78.067 | β = 90 |
| c = 78.067 | γ = 90 |
| Software Name | Purpose |
|---|---|
| Aimless | data scaling |
| PHENIX | refinement |
| PDB_EXTRACT | data extraction |
| PHASER | phasing |
| XDS | data reduction |
Entry History & Funding Information
Deposition Data
- Released Date: 2018-02-21 Deposition Author(s): Lieblich, S.A., Fang, K.Y., Tirrell, D.A.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Novo Nordisk Foundation | Denmark | -- |
Revision History (Full details and data files)
- Version 1.0: 2018-02-21
Type: Initial release - Version 1.1: 2020-01-15
Changes: Author supporting evidence - Version 1.2: 2023-10-04
Changes: Data collection, Database references, Refinement description
