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PDBsum entry 3mzw
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protein ligands Protein-protein interface(s) links
Transferase PDB id
3mzw

 

 

 

 

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Contents
Protein chains
569 a.a. *
53 a.a. *
Ligands
NAG-NAG
NAG ×2
Waters ×9
* Residue conservation analysis
PDB id:
3mzw
Name: Transferase
Title: Her2 extracelluar region with affinity matured 3-helix affibody zher2:342
Structure: Tyrosine kinase-type cell surface receptor her2. Chain: a. Fragment: extracellular domain residues 23-646. Synonym: receptor tyrosine-protein kinase erbb-2, p185erbb2, proto- oncogenE C-erbb-2, proto-oncogene neu, metastatic lymph node gene 19 protein, mln 19. Engineered: yes. Immunoglobulin g-binding protein a. Chain: b.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: erbb2, her2, mln19, neu, ngl. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Synthetic: yes. Staphylococcus aureus. Organism_taxid: 1280.
Resolution:
2.90Å     R-factor:   0.208     R-free:   0.278
Authors: C.Eigenbrot,M.H.Ultsch
Key ref: C.Eigenbrot et al. (2010). Structural basis for high-affinity HER2 receptor binding by an engineered protein. Proc Natl Acad Sci U S A, 107, 15039-15044. PubMed id: 20696930
Date:
13-May-10     Release date:   28-Jul-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
P04626  (ERBB2_HUMAN) -  Receptor tyrosine-protein kinase erbB-2 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1255 a.a.
569 a.a.
Protein chain
P38507  (SPA_STAAU) -  Immunoglobulin G-binding protein A from Staphylococcus aureus
Seq:
Struc: 		508 a.a.
53 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 13 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.2.7.10.1  - receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
L-tyrosyl-[protein]
 + ATP
 = O-phospho-L-tyrosyl-[protein]
Bound ligand (Het Group name = NAG)
matches with 41.38% similarity 		+ ADP
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Proc Natl Acad Sci U S A 107:15039-15044 (2010)
PubMed id: 20696930  
 
 
Structural basis for high-affinity HER2 receptor binding by an engineered protein.
C.Eigenbrot, M.Ultsch, A.Dubnovitsky, L.Abrahmsén, T.Härd.
 
  ABSTRACT  
 
No abstract given.

 

 

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