Download Mendeleycrystal structure of EFI target 500140:TatD family hydrolase from Pseudomonas putida
Kim, J., Toro, R., Hillerich, B., Seidel, R.D., Gerlt, J.A., Almo, S.C., Enzyme Function Initiative (EFI)To be published.
3RCM
crystal structure of EFI target 500140:TatD family hydrolase from Pseudomonas putida
- PDB DOI: https://doi.org/10.2210/pdb3RCM/pdb
- Classification: HYDROLASE
- Organism(s): Pseudomonas putida KT2440
- Expression System: Escherichia coli BL21
- Mutation(s): No
- Deposited: 2011-03-31 Released: 2011-04-20
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.05 Å
- R-Value Free: 0.226
- R-Value Work: 0.172
- R-Value Observed: 0.175
wwPDB Validation 3D Report Full Report
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 |
| TatD family hydrolase | 287 | Pseudomonas putida KT2440 | Mutation(s): 0 Gene Names: PP2311, PP_2311 |  | |
UniProt | |||||
Find proteins for Q88KH9 (Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)) Explore Q88KH9 Go to UniProtKB: Q88KH9 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q88KH9 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| CIT Query on CIT | C [auth A] | CITRIC ACID C6 H8 O7 KRKNYBCHXYNGOX-UHFFFAOYSA-N |  | ||
| ZN Query on ZN | B [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
| ACT Query on ACT | D [auth A] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-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: 2.05 Å
- R-Value Free: 0.226
- R-Value Work: 0.172
- R-Value Observed: 0.175
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 51.007 | α = 90 |
| b = 62.643 | β = 90 |
| c = 88.57 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| SOLVE | phasing |
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2011-04-20 Deposition Author(s): Kim, J., Toro, R., Hillerich, B., Seidel, R.D., Gerlt, J.A., Almo, S.C., Enzyme Function Initiative (EFI)
Revision History (Full details and data files)
- Version 1.0: 2011-04-20
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2018-01-24
Changes: Database references
