Download MendeleyFatty acid ABC transporter substrate-binding protein from Thermomonospora curvata
Osipiuk, J., Li, H., Endres, M., Joachimiak, A.To be published.
4N03
Fatty acid ABC transporter substrate-binding protein from Thermomonospora curvata
- PDB DOI: https://doi.org/10.2210/pdb4N03/pdb
- Classification: TRANSPORT PROTEIN
- Organism(s): Thermomonospora curvata DSM 43183
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2013-09-30 Released: 2013-10-16
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.15 ?
- R-Value Free: 0.149
- R-Value Work: 0.124
- R-Value Observed: 0.125
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 |
| ABC-type branched-chain amino acid transport systems periplasmic component-like protein | 405 | Thermomonospora curvata DSM 43183 | Mutation(s): 0 Gene Names: NC_013510.1:3663026..3664297, Tcur_3166 |  | |
UniProt | |||||
Find proteins for D1A9M1 (Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9)) Explore D1A9M1 Go to UniProtKB: D1A9M1 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | D1A9M1 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PLM Query on PLM | B [auth A] | PALMITIC ACID C16 H32 O2 IPCSVZSSVZVIGE-UHFFFAOYSA-N |  | ||
| EDO Query on EDO | C [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-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: 1.15 ?
- R-Value Free: 0.149
- R-Value Work: 0.124
- R-Value Observed: 0.125
- Space Group: P 1 21 1
- Diffraction Data: https://doi.org/10.18430/M34N03
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 63.409 | ¦Á = 90 |
| b = 40.303 | ¦Â = 90.6 |
| c = 72.557 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| DENZO | data reduction |
| SCALEPACK | data scaling |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| SBC-Collect | data collection |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| SHELXD | phasing |
| MLPHARE | phasing |
| DM | phasing |
| SOLVE | phasing |
| RESOLVE | phasing |
| HKL-3000 | phasing |
Entry History
Deposition Data
- Released Date: 2013-10-16 Deposition Author(s): Osipiuk, J., Li, H., Endres, M., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2013-10-16
Type: Initial release - Version 1.1: 2017-11-15
Changes: Refinement description - Version 1.2: 2024-10-16
Changes: Data collection, Database references, Derived calculations, Structure summary
