4FKE
Crystal structure of porcine aminopeptidase-N
- PDB DOI: https://doi.org/10.2210/pdb4FKE/pdb
- Classification: HYDROLASE
- Organism(s): Sus scrofa
- Expression System: Spodoptera frugiperda
- Mutation(s): No 
- Deposited: 2012-06-13 Released: 2012-10-17 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.85 Å
- R-Value Free: 0.182 
- R-Value Work: 0.142 
- R-Value Observed: 0.144 
This is version 2.0 of the entry. See complete history. 
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
Aminopeptidase N | 909 | Sus scrofa | Mutation(s): 0  Gene Names: ANPEP EC: 3.4.11.2 | ||
UniProt | |||||
Find proteins for P15145 (Sus scrofa) Explore P15145  Go to UniProtKB:  P15145 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P15145 | ||||
Sequence AnnotationsExpand | |||||
|
Oligosaccharides
Entity ID: 2 | |||||
---|---|---|---|---|---|
Molecule | Chains | Length | 2D Diagram | Glycosylation | 3D Interactions |
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | B, C, F | 3 | N-Glycosylation | ||
Glycosylation Resources | |||||
GlyTouCan:  G47362BJ GlyCosmos:  G47362BJ GlyGen:  G47362BJ |
Small Molecules
Ligands 2 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
NAG Query on NAG | K [auth A], L [auth A] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N | |||
ZN Query on ZN | M [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |
Biologically Interesting Molecules (External Reference) 1 Unique
Entity ID: 2 | |||||
---|---|---|---|---|---|
ID | Chains | Name | Type/Class | 2D Diagram | 3D Interactions |
PRD_900017 Query on PRD_900017 | B, C, F | triacetyl-beta-chitotriose | Oligosaccharide / Inhibitor |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.85 Å
- R-Value Free: 0.182 
- R-Value Work: 0.142 
- R-Value Observed: 0.144 
- Space Group: C 1 2 1
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 259.971 | α = 90 |
b = 62.77 | β = 100.12 |
c = 81.794 | γ = 90 |
Software Name | Purpose |
---|---|
REFMAC | refinement |
SOLVE | phasing |
CNS | refinement |
HKL-2000 | data reduction |
HKL-2000 | data scaling |
HKL-2000 | data collection |
Entry History 
Deposition Data
Revision History (Full details and data files)
- Version 1.0: 2012-10-17
Type: Initial release - Version 1.1: 2012-10-31
Changes: Database references, Structure summary - Version 1.2: 2012-11-14
Changes: Database references - Version 1.3: 2019-07-17
Changes: Data collection, Derived calculations, Refinement description - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Structure summary