Download MendeleyThe Structures of the Phycobiliproteins of Gloeobacter Violaceus
Murray, J.W., Benson, S., Nield, J., Barber, J.To be published.
2VJH
The structure of Phycoerythrin from Gloeobacter violaceus
- PDB DOI: https://doi.org/10.2210/pdb2VJH/pdb
- Classification: PHOTOSYNTHESIS
- Organism(s): Gloeobacter violaceus
- Mutation(s): No
- Deposited: 2007-12-10 Released: 2008-03-25
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 ?
- R-Value Free: 0.186
- R-Value Work: 0.153
- R-Value Observed: 0.155
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 |
| PHYCOERYTHRIN ALPHA CHAIN | 164 | Gloeobacter violaceus | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for Q7NLD7 (Gloeobacter violaceus (strain ATCC 29082 / PCC 7421)) Explore Q7NLD7 Go to UniProtKB: Q7NLD7 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q7NLD7 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| PHYCOERYTHRIN BETA SUBUNIT | 177 | Gloeobacter violaceus | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for Q7NLD6 (Gloeobacter violaceus (strain ATCC 29082 / PCC 7421)) Explore Q7NLD6 Go to UniProtKB: Q7NLD6 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q7NLD6 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PUB Query on PUB | G [auth B], L [auth D] | PHYCOUROBILIN C33 H42 N4 O6 KDCCOOGTVSRCHX-YYVBKQGDSA-N |  | ||
| PEB Query on PEB | E [auth A] F [auth A] H [auth B] I [auth B] J [auth C] | PHYCOERYTHROBILIN C33 H40 N4 O6 NKCBCVIFPXGHAV-WAVSMFBNSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MEN Query on MEN | B, D | L-PEPTIDE LINKING | C5 H10 N2 O3 |  | ASN |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 ?
- R-Value Free: 0.186
- R-Value Work: 0.153
- R-Value Observed: 0.155
- Space Group: P 21 3
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 155.829 | ¦Á = 90 |
| b = 155.829 | ¦Â = 90 |
| c = 155.829 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| MOSFLM | data reduction |
| SCALA | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2008-03-25 Deposition Author(s): Murray, J.W., Benson, S., Nield, J., Barber, J.
Revision History (Full details and data files)
- Version 1.0: 2008-03-25
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Refinement description, Version format compliance - Version 1.2: 2023-12-13
Changes: Data collection, Database references, Derived calculations, Other, Refinement description
