Download MendeleyThe role of the active site Zn in the catalytic mechanism of the GH38 Golgi alpha-mannosidase II: implications from noeuromycin inhibition
Kuntz, D.A., Liu, H., Bols, M., Rose, D.R.(2006) Biocatal Biotransformation 34: 55-61
2ALW
Golgi alpha-mannosidase II complex with Noeuromycin
- PDB DOI: https://doi.org/10.2210/pdb2ALW/pdb
- Classification: HYDROLASE
- Organism(s): Drosophila melanogaster
- Expression System: Drosophila melanogaster
- Mutation(s): Yes
- Deposited: 2005-08-08 Released: 2006-07-04
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.86 Å
- R-Value Free: 0.181
- R-Value Work: 0.141
- R-Value Observed: 0.141
Starting Model: experimental
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This is version 1.5 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Alpha-mannosidase II | 1,045 | Drosophila melanogaster | Mutation(s): 1 Gene Names: GmII EC: 3.2.1.114 |  | |
UniProt | |||||
Find proteins for Q24451 (Drosophila melanogaster) Explore Q24451 Go to UniProtKB: Q24451 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q24451 | ||||
Glycosylation | |||||
| Glycosylation Sites: 1 | Go to GlyGen: Q24451-1 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAG Query on NAG | B [auth A] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N |  | ||
| MNM Query on MNM | D [auth A] | (2S,3S,4R,5R)-2,3,4-TRIHYDROXY-5-HYDROXYMETHYL-PIPERIDINE C6 H13 N O4 BHOYFRIRWXBNHP-ZXXMMSQZSA-N |  | ||
| MPD Query on MPD | E [auth A] | (4S)-2-METHYL-2,4-PENTANEDIOL C6 H14 O2 SVTBMSDMJJWYQN-YFKPBYRVSA-N |  | ||
| ZN Query on ZN | C [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.86 Å
- R-Value Free: 0.181
- R-Value Work: 0.141
- R-Value Observed: 0.141
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 68.502 | α = 90 |
| b = 109.19 | β = 90 |
| c = 138.148 | γ = 90 |
| Software Name | Purpose |
|---|---|
| CNS | refinement |
| DENZO | data reduction |
| SCALEPACK | data scaling |
| CNS | phasing |
Entry History
Deposition Data
- Released Date: 2006-07-04 Deposition Author(s): Kuntz, D.A., Bols, M.B., Liu, H., Rose, D.R.
Revision History (Full details and data files)
- Version 1.0: 2006-07-04
Type: Initial release - Version 1.1: 2008-04-30
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Non-polymer description, Version format compliance - Version 1.3: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Data collection, Database references, Derived calculations, Structure summary - Version 1.4: 2023-08-23
Changes: Data collection, Database references, Refinement description, Structure summary - Version 1.5: 2024-11-06
Changes: Structure summary
