Download MendeleyCrystal structure of Putative lipid binding protein (NP_811174.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 2.20 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3H3I
CRYSTAL STRUCTURE OF A PUTATIVE LIPID BINDING PROTEIN (BT_2261) FROM BACTEROIDES THETAIOTAOMICRON VPI-5482 AT 2.20 A RESOLUTION
- PDB DOI: https://doi.org/10.2210/pdb3H3I/pdb
- Classification: LIPID BINDING PROTEIN
- Organism(s): Bacteroides thetaiotaomicron VPI-5482
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2009-04-16 Released: 2009-04-28
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.232
- R-Value Work: 0.187
- R-Value Observed: 0.189
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 lipid binding protein | 150 | Bacteroides thetaiotaomicron VPI-5482 | Mutation(s): 0 Gene Names: BT_2261, NP_811174.1 |  | |
UniProt | |||||
Find proteins for Q8A5H8 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)) Explore Q8A5H8 Go to UniProtKB: Q8A5H8 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8A5H8 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 Query on SO4 | D [auth A] E [auth B] F [auth B] G [auth C] H [auth C] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C | 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: 0.232
- R-Value Work: 0.187
- R-Value Observed: 0.189
- Space Group: P 32 1 2
- Diffraction Data: https://doi.org/10.18430/M33H3I
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 67.383 | α = 90 |
| b = 67.383 | β = 90 |
| c = 186.164 | γ = 120 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SHELX | phasing |
| MolProbity | model building |
| SCALA | data scaling |
| PDB_EXTRACT | data extraction |
| MOSFLM | data reduction |
| SHELXD | phasing |
| autoSHARP | phasing |
Entry History
Deposition Data
- Released Date: 2009-04-28 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2009-04-28
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: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-02-01
Changes: Database references, Derived calculations
