Download MendeleyCrystal structure of Putative serine hydrolase (NP_639225.1) from XANTHOMONAS CAMPESTRIS at 2.69 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3KSR
CRYSTAL STRUCTURE OF A PUTATIVE SERINE HYDROLASE (XCC3885) FROM XANTHOMONAS CAMPESTRIS PV. CAMPESTRIS AT 2.69 A RESOLUTION
- PDB DOI: https://doi.org/10.2210/pdb3KSR/pdb
- Classification: HYDROLASE
- Organism(s): Xanthomonas campestris pv. campestris str. ATCC 33913
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2009-11-23 Released: 2009-12-22
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.69 Å
- R-Value Free: 0.222
- R-Value Work: 0.197
- R-Value Observed: 0.198
wwPDB Validation 3D Report Full Report
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 |
| Putative serine hydrolase | 290 | Xanthomonas campestris pv. campestris str. ATCC 33913 | Mutation(s): 0 Gene Names: XCC3885 |  | |
UniProt | |||||
Find proteins for Q8P431 (Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)) Explore Q8P431 Go to UniProtKB: Q8P431 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8P431 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PO4 Query on PO4 | B [auth A], C [auth A] | PHOSPHATE ION O4 P NBIIXXVUZAFLBC-UHFFFAOYSA-K |  | ||
| CL Query on CL | D [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| 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: 2.69 Å
- R-Value Free: 0.222
- R-Value Work: 0.197
- R-Value Observed: 0.198
- Space Group: P 43 21 2
- Diffraction Data: https://doi.org/10.18430/M33KSR
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 56.865 | α = 90 |
| b = 56.865 | β = 90 |
| c = 220.25 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SHELX | phasing |
| MolProbity | model building |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
| XDS | data reduction |
| SHELXD | phasing |
| autoSHARP | phasing |
Entry History
Deposition Data
- Released Date: 2009-12-22 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2009-12-22
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2017-11-01
Changes: Refinement description - Version 1.3: 2019-07-17
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-02-01
Changes: Database references, Derived calculations
