1NQL
Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in an inactive (low pH) complex with EGF.
- PDB DOI: https://doi.org/10.2210/pdb1NQL/pdb
- Classification: HORMONE/GROWTH FACTOR RECEPTOR
- Organism(s): Homo sapiens
- Expression System: Spodoptera frugiperda, Escherichia coli
- Mutation(s): No 
- Deposited: 2003-01-21 Released: 2003-03-11 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.80 Å
- R-Value Free: 0.310 
- R-Value Work: 0.241 
- R-Value Observed: 0.247 
wwPDB Validation   3D Report Full Report
This is version 2.1 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 |
epidermal growth factor receptor | 624 | Homo sapiens | Mutation(s): 0  | ||
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P00533 (Homo sapiens) Explore P00533  Go to UniProtKB:  P00533 | |||||
PHAROS:  P00533 GTEx:  ENSG00000146648  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P00533 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
epidermal growth factor | 53 | Homo sapiens | Mutation(s): 0  Gene Names: EGF | ||
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P01133 (Homo sapiens) Explore P01133  Go to UniProtKB:  P01133 | |||||
PHAROS:  P01133 GTEx:  ENSG00000138798  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P01133 | ||||
Sequence AnnotationsExpand | |||||
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Oligosaccharides
Small Molecules
Ligands 1 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
NAG Query on NAG | F [auth A], G [auth A], H [auth A], I [auth A], J [auth A] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.80 Å
- R-Value Free: 0.310 
- R-Value Work: 0.241 
- R-Value Observed: 0.247 
- Space Group: C 1 2 1
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 119.17 | α = 90 |
b = 103.66 | β = 119.27 |
c = 101.49 | γ = 90 |
Software Name | Purpose |
---|---|
REFMAC | refinement |
MOSFLM | data reduction |
CCP4 | data scaling |
AMoRE | phasing |
Entry History 
Deposition Data
- Released Date: 2003-03-11  Deposition Author(s): Ferguson, K.M., Lemmon, M.A.
Revision History (Full details and data files)
- Version 1.0: 2003-03-11
Type: Initial release - Version 1.1: 2008-04-29
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Non-polymer description, Version format compliance - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Atomic model, Data collection, Derived calculations, Structure summary - Version 2.1: 2023-08-16
Changes: Advisory, Data collection, Database references, Refinement description, Structure summary