Download MendeleyCrystal structure of protein of unknown function (DUF692/COG3220) (YP_719350.1) from Haemophilus somnus 129PT at 2.20 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3BWW | pdb_00003bww
Crystal structure of a duf692 family protein (hs_1138) from haemophilus somnus 129pt at 2.20 A resolution
- PDB DOI: https://doi.org/10.2210/pdb3BWW/pdb
- Classification: METAL BINDING PROTEIN
- Organism(s): Histophilus somni 129PT
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2008-01-10 Released: 2008-01-22
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.260 (Depositor), 0.260 (DCC)
- R-Value Work: 0.195 (Depositor), 0.200 (DCC)
- R-Value Observed: 0.198 (Depositor)
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 DUF692/COG3220 | 307 | Histophilus somni 129PT | Mutation(s): 0 Gene Names: YP_719350.1, HS_1138 |  | |
UniProt | |||||
Find proteins for Q0I408 (Histophilus somni (strain 129Pt)) Explore Q0I408 Go to UniProtKB: Q0I408 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q0I408 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| CAC Query on CAC | D [auth A] | CACODYLATE ION C2 H6 As O2 OGGXGZAMXPVRFZ-UHFFFAOYSA-M |  | ||
| EDO Query on EDO | E [auth A], F [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| FE Query on FE | B [auth A], C [auth A] | FE (III) ION Fe VTLYFUHAOXGGBS-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: 2.20 Å
- R-Value Free: 0.260 (Depositor), 0.260 (DCC)
- R-Value Work: 0.195 (Depositor), 0.200 (DCC)
- R-Value Observed: 0.198 (Depositor)
Diffraction Data: https://doi.org/10.18430/M33BWW
Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 53.572 | α = 90 |
| b = 65.992 | β = 90 |
| c = 95.585 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SOLVE | phasing |
| MolProbity | model building |
| SCALA | data scaling |
| PDB_EXTRACT | data extraction |
| MAR345 | data collection |
| MOSFLM | data reduction |
Entry History
Deposition Data
- Released Date: 2008-01-22 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2008-01-22
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Source and taxonomy, Version format compliance - Version 1.2: 2017-10-25
Changes: Refinement description - Version 1.3: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-01-25
Changes: Database references, Derived calculations - Version 1.5: 2024-11-20
Changes: Data collection, Structure summary
