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 | |||||
|---|---|---|---|---|---|
| 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
