1IVO
Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains.
- PDB DOI: https://doi.org/10.2210/pdb1IVO/pdb
- Classification: TRANSFERASE/SIGNALING PROTEIN
- Organism(s): Homo sapiens
- Expression System: Cricetulus griseus, Escherichia coli
- Mutation(s): No 
- Deposited: 2002-03-28 Released: 2002-10-16 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 3.30 Å
- R-Value Free: 0.326 
- R-Value Work: 0.255 
- R-Value Observed: 0.258 
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 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
Epidermal Growth Factor Receptor | 622 | Homo sapiens | Mutation(s): 0  EC: 2.7.1.112 | ||
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  | ||
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: 3.30 Å
- R-Value Free: 0.326 
- R-Value Work: 0.255 
- R-Value Observed: 0.258 
- Space Group: P 31 2 1
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 220.164 | α = 90 |
b = 220.164 | β = 90 |
c = 113.121 | γ = 120 |
Software Name | Purpose |
---|---|
DENZO | data reduction |
SCALEPACK | data scaling |
MLPHARE | phasing |
CNS | refinement |
Entry History 
Deposition Data
- Released Date: 2002-10-16  Deposition Author(s): Ogiso, H., Ishitani, R., Nureki, O., Fukai, S., Yamanaka, M., Kim, J.H., Saito, K., Shirouzu, M., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Revision History (Full details and data files)
- Version 1.0: 2002-10-16
Type: Initial release - Version 1.1: 2008-04-27
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: 2023-12-27
Changes: Advisory, Data collection, Database references, Structure summary