Download MendeleyCrystal Structure of FolD Bifunctional Protein from
Kim, Y., Zhang, R., Makowska-Grzyska, M., Papazisi, L., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)To be published.
3P2O | pdb_00003p2o
Crystal Structure of FolD Bifunctional Protein from Campylobacter jejuni
- PDB DOI: https://doi.org/10.2210/pdb3P2O/pdb
- Classification: OXIDOREDUCTASE, HYDROLASE
- Organism(s): Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2010-10-03 Released: 2010-10-13
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.23 Å
- R-Value Free: 0.254 (Depositor), 0.250 (DCC)
- R-Value Work: 0.189 (Depositor), 0.180 (DCC)
- R-Value Observed: 0.193 (Depositor)
Starting Model: experimental
View more details
This is version 1.3 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 |
| Bifunctional protein folD | 285 | Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819 | Mutation(s): 0 Gene Names: Cj0855, folD EC: 1.5.1.5 (PDB Primary Data), 3.5.4.9 (PDB Primary Data) |  | |
UniProt | |||||
Find proteins for Q0PA35 (Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)) Explore Q0PA35 Go to UniProtKB: Q0PA35 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q0PA35 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAD Query on NAD | C [auth A], E [auth B] | NICOTINAMIDE-ADENINE-DINUCLEOTIDE C21 H27 N7 O14 P2 BAWFJGJZGIEFAR-NNYOXOHSSA-N |  | ||
| GOL Query on GOL | D [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.23 Å
- R-Value Free: 0.254 (Depositor), 0.250 (DCC)
- R-Value Work: 0.189 (Depositor), 0.180 (DCC)
- R-Value Observed: 0.193 (Depositor)
Diffraction Data: https://doi.org/10.18430/m33p2o
Space Group: C 1 2 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 134.927 | α = 90 |
| b = 44.981 | β = 119.84 |
| c = 117.021 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| HKL-3000 | data collection |
| HKL-3000 | phasing |
| MOLREP | phasing |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
Entry History
Deposition Data
- Released Date: 2010-10-13 Deposition Author(s): Kim, Y., Zhang, R., Makowska-Grzyska, M., Papazisi, L., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)
Revision History (Full details and data files)
- Version 1.0: 2010-10-13
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2024-04-03
Changes: Data collection, Database references, Derived calculations, Refinement description - Version 1.3: 2024-11-06
Changes: Structure summary
