Download MendeleyCrystal structure of S-adenosyl-L-homocysteine hydrolase from brucella melitensis in ternary complex with NAD and adenosine, orthorhombic form
SSGCID, Gardberg, A., Sankaran, B., Abendroth, J., Staker, B.To be published.
3N58
Crystal structure of S-ADENOSYL-L-HOMOCYSTEINE hydrolase from brucella melitensis in ternary complex with NAD and adenosine, orthorhombic form
- PDB DOI: https://doi.org/10.2210/pdb3N58/pdb
- Classification: HYDROLASE
- Organism(s): Brucella abortus 2308
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2010-05-24 Released: 2010-06-02
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.39 ?
- R-Value Free: 0.235
- R-Value Work: 0.172
- R-Value Observed: 0.175
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 |
| Adenosylhomocysteinase | 464 | Brucella abortus 2308 | Mutation(s): 0 Gene Names: ahcY, BAB1_2099 EC: 3.3.1.1 (PDB Primary Data), 3.13.2.1 (UniProt) |  | |
UniProt | |||||
Find proteins for Q2YQX8 (Brucella abortus (strain 2308)) Explore Q2YQX8 Go to UniProtKB: Q2YQX8 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q2YQX8 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAD Query on NAD | G [auth A], H [auth B], K [auth C], N [auth D] | NICOTINAMIDE-ADENINE-DINUCLEOTIDE C21 H27 N7 O14 P2 BAWFJGJZGIEFAR-NNYOXOHSSA-N |  | ||
| ADN Query on ADN | F [auth A], J [auth C], M [auth D] | ADENOSINE C10 H13 N5 O4 OIRDTQYFTABQOQ-KQYNXXCUSA-N |  | ||
| K Query on K | E [auth A], I [auth C], L [auth D] | POTASSIUM ION K NPYPAHLBTDXSSS-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.39 ?
- R-Value Free: 0.235
- R-Value Work: 0.172
- R-Value Observed: 0.175
- Space Group: P 21 21 21
- Diffraction Data: https://doi.org/10.18430/M33N58
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 68.45 | ¦Á = 90 |
| b = 165.23 | ¦Â = 90 |
| c = 184.14 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| ADSC | data collection |
| PHASER | phasing |
| PHENIX | refinement |
| XDS | data reduction |
| XSCALE | data scaling |
Entry History
Deposition Data
- Released Date: 2010-06-02 Deposition Author(s): Seattle Structural Genomics Center for Infectious Disease (SSGCID)
Revision History (Full details and data files)
- Version 1.0: 2010-06-02
Type: Initial release - Version 1.1: 2011-07-13
Changes: Source and taxonomy, Version format compliance - Version 1.2: 2012-03-21
Changes: Refinement description - Version 1.3: 2018-01-24
Changes: Database references - Version 1.4: 2023-09-06
Changes: Data collection, Database references, Derived calculations, Refinement description
