Download MendeleyCrystal structure of Rossmann-fold protein of unknown function (DUF574) (NP_823353.1) from Streptomyces avermitilis MA-4680 at 1.45 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3GIW
CRYSTAL STRUCTURE OF a DUF574 family protein (SAV_2177) FROM STREPTOMYCES AVERMITILIS MA-4680 AT 1.45 A RESOLUTION
- PDB DOI: https://doi.org/10.2210/pdb3GIW/pdb
- Classification: UNKNOWN FUNCTION
- Organism(s): Streptomyces avermitilis MA-4680 = NBRC 14893
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2009-03-06 Released: 2009-04-14
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.45 Å
- R-Value Free: 0.176
- R-Value Work: 0.156
- R-Value Observed: 0.157
wwPDB Validation 3D Report Full Report
This is version 1.5 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 |
| Protein of unknown function DUF574 | 277 | Streptomyces avermitilis MA-4680 = NBRC 14893 | Mutation(s): 0 Gene Names: NP_823353.1, SAV2177, SAV_2177 |  | |
UniProt | |||||
Find proteins for Q82L35 (Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)) Explore Q82L35 Go to UniProtKB: Q82L35 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q82L35 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | C [auth A], D [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| UNL Query on UNL | B [auth A] | Unknown ligand PEDCQBHIVMGVHV-UHFFFAOYSA-N | |||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.45 Å
- R-Value Free: 0.176
- R-Value Work: 0.156
- R-Value Observed: 0.157
- Space Group: C 1 2 1
- Diffraction Data: https://doi.org/10.18430/M33GIW
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 129.716 | α = 90 |
| b = 49.669 | β = 94.72 |
| c = 45.132 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SHELX | phasing |
| MolProbity | model building |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
| MAR345 | data collection |
| XDS | data reduction |
| SHELXD | phasing |
| autoSHARP | phasing |
Entry History
Deposition Data
- Released Date: 2009-04-14 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2009-04-14
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Source and taxonomy, Version format compliance - Version 1.2: 2017-11-01
Changes: Refinement description - Version 1.3: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-02-01
Changes: Database references, Derived calculations - Version 1.5: 2024-10-09
Changes: Data collection, Structure summary
