Download MendeleyCrystal structure of PH1503 protein from Pyrococcus Horikoshii OT3
Bagautdinov, B., Kunishima, N.To be published.
2DCL | pdb_00002dcl
Structure of PH1503 protein from Pyrococcus Horikoshii OT3
- PDB DOI: https://doi.org/10.2210/pdb2DCL/pdb
- Classification: Structural genomics, unknown function
- Organism(s): Pyrococcus horikoshii
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2006-01-08 Released: 2006-07-08
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.28 Å
- R-Value Free: 0.290 (Depositor), 0.290 (DCC)
- R-Value Work: 0.244 (Depositor), 0.240 (DCC)
- R-Value Observed: 0.244 (Depositor)
Starting Model: experimental
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This is version 1.4 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 |
| Hypothetical UPF0166 protein PH1503 | 127 | Pyrococcus horikoshii | Mutation(s): 0 Gene Names: PH1503 |  | |
UniProt | |||||
Find proteins for O59172 (Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)) Explore O59172 Go to UniProtKB: O59172 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | O59172 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| AMP Query on AMP | D [auth A], E [auth B], F [auth B] | ADENOSINE MONOPHOSPHATE C10 H14 N5 O7 P UDMBCSSLTHHNCD-KQYNXXCUSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.28 Å
- R-Value Free: 0.290 (Depositor), 0.290 (DCC)
- R-Value Work: 0.244 (Depositor), 0.240 (DCC)
- R-Value Observed: 0.244 (Depositor)
Space Group: C 1 2 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 107.562 | α = 90 |
| b = 59.647 | β = 122.47 |
| c = 66.738 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| SCALEPACK | data scaling |
| CNS | refinement |
| HKL-2000 | data reduction |
| CNS | phasing |
Entry History
Deposition Data
- Released Date: 2006-07-08 Deposition Author(s): Bagautdinov, B., Kunishima, N., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Revision History (Full details and data files)
- Version 1.0: 2006-07-08
Type: Initial release - Version 1.1: 2008-04-30
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Derived calculations, Version format compliance - Version 1.3: 2019-12-25
Changes: Data collection - Version 1.4: 2023-10-25
Changes: Data collection, Database references, Derived calculations, Refinement description
