Download MendeleyCrystal structure of a FAD binding protein from Bacillus cereus, a putative NAD(FAD)-utilizing dehydrogenases
Minasov, G., Shuvalova, L., Vorontsov, I.I., Kiryukhina, O., Abdullah, J., Collart, F.R., Joachimiak, A., Anderson, W.F.To be published.
2I0Z | pdb_00002i0z
Crystal structure of a FAD binding protein from Bacillus cereus, a putative NAD(FAD)-utilizing dehydrogenases
- PDB DOI: https://doi.org/10.2210/pdb2I0Z/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Bacillus cereus
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2006-08-11 Released: 2006-08-22
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.84 Å
- R-Value Free: 0.248 (Depositor), 0.240 (DCC)
- R-Value Work: 0.195 (Depositor), 0.190 (DCC)
- R-Value Observed: 0.198 (Depositor)
Starting Model: experimental
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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 |
| NAD(FAD)-utilizing dehydrogenases | 447 | Bacillus cereus | Mutation(s): 1 Gene Names: BC_4706 |  | |
UniProt | |||||
Find proteins for Q816V9 (Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)) Explore Q816V9 Go to UniProtKB: Q816V9 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q816V9 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| FAD Query on FAD | C [auth A] | FLAVIN-ADENINE DINUCLEOTIDE C27 H33 N9 O15 P2 VWWQXMAJTJZDQX-UYBVJOGSSA-N |  | ||
| CL Query on CL | B [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.84 Å
- R-Value Free: 0.248 (Depositor), 0.240 (DCC)
- R-Value Work: 0.195 (Depositor), 0.190 (DCC)
- R-Value Observed: 0.198 (Depositor)
Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 46.716 | α = 90 |
| b = 92.366 | β = 90 |
| c = 97.504 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| Blu-Ice | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| PHASER | phasing |
Entry History
Deposition Data
- Released Date: 2006-08-22 Deposition Author(s): Minasov, G., Shuvalova, L., Vorontsov, I.I., Kiryukhina, O., Abdullah, J., Collart, F.R., Joachimiak, A., Anderson, W.F., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2006-08-22
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2021-10-20
Changes: Database references, Derived calculations - Version 1.4: 2023-08-30
Changes: Data collection, Refinement description
