4GQQ
Human pancreatic alpha-amylase with bound ethyl caffeate
- PDB DOI: https://doi.org/10.2210/pdb4GQQ/pdb
- Classification: HYDROLASE/HYDROLASE INHIBITOR
- Organism(s): Homo sapiens
- Expression System: Komagataella pastoris
- Mutation(s): No 
- Deposited: 2012-08-23 Released: 2012-10-24 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.35 Å
- R-Value Free: 0.227 
- R-Value Work: 0.197 
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 |
Pancreatic alpha-amylase | 496 | Homo sapiens | Mutation(s): 0  Gene Names: AMY2A EC: 3.2.1.1 | ||
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P04746 (Homo sapiens) Explore P04746  Go to UniProtKB:  P04746 | |||||
PHAROS:  P04746 GTEx:  ENSG00000243480  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P04746 | ||||
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 | |||
0XR Query on 0XR | C [auth A], D [auth A], E [auth A] | ethyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate C11 H12 O4 WDKYDMULARNCIS-GQCTYLIASA-N | |||
CA Query on CA | G [auth A] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N | |||
CL Query on CL | F [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |
Modified Residues 1 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Type | Formula | 2D Diagram | Parent |
PCA Query on PCA | A | L-PEPTIDE LINKING | C5 H7 N O3 | GLN |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.35 Å
- R-Value Free: 0.227 
- R-Value Work: 0.197 
- Space Group: P 21 21 21
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 52.06 | α = 90 |
b = 68.12 | β = 90 |
c = 125.91 | γ = 90 |
Software Name | Purpose |
---|---|
Web-Ice | data collection |
CNS | refinement |
MOSFLM | data reduction |
SCALA | data scaling |
CNS | phasing |
Entry History 
Deposition Data
- Released Date: 2012-10-24  Deposition Author(s): Williams, L.K., Brayer, G.D.
Revision History (Full details and data files)
- Version 1.0: 2012-10-24
Type: Initial release - Version 1.1: 2012-12-12
Changes: Database references - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Derived calculations, Polymer sequence, Refinement description, Structure summary