Download MendeleyUDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - BH2 complex form
Killivalavan, A., Lee, K.H.To be published.
5ZER
UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - BH2 complex form
- PDB DOI: https://doi.org/10.2210/pdb5ZER/pdb
- Classification: TRANSFERASE
- Organism(s): Synechococcus elongatus PCC 7942 = FACHB-805
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2018-02-27 Released: 2019-03-06
- Funding Organization(s): National Research Foundation (Korea)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.39 Å
- R-Value Free: 0.286
- R-Value Work: 0.215
- R-Value Observed: 0.219
Starting Model: experimental
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This is version 1.2 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| UDP-glucose:tetrahydrobiopterin glucosyltransferase | 354 | Synechococcus elongatus PCC 7942 = FACHB-805 | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for Q31LX1 (Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)) Explore Q31LX1 Go to UniProtKB: Q31LX1 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q31LX1 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| HBI (Subject of Investigation/LOI) Query on HBI | C [auth A], E [auth B] | 7,8-DIHYDROBIOPTERIN C9 H13 N5 O3 FEMXZDUTFRTWPE-DZSWIPIPSA-N |  | ||
| GOL Query on GOL | D [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.39 Å
- R-Value Free: 0.286
- R-Value Work: 0.215
- R-Value Observed: 0.219
- Space Group: C 1 2 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 167.13 | α = 90 |
| b = 80 | β = 91.27 |
| c = 53.38 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| MOLREP | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2019-03-06 Deposition Author(s): Killivalavan, A., Lee, K.H.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Research Foundation (Korea) | Korea, Republic Of | NRF-2012R1A1A2044394 |
Revision History (Full details and data files)
- Version 1.0: 2019-03-06
Type: Initial release - Version 1.1: 2023-11-22
Changes: Data collection, Database references, Refinement description - Version 1.2: 2024-11-20
Changes: Structure summary
