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PDBsum entry 3bin

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protein ligands links
Cell adhesion PDB id
3bin

 

 

 

 

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Contents
Protein chain
281 a.a. *
Ligands
GLY-THR-TYR-PHE-
THR-HIS-GLU
Waters ×144
* Residue conservation analysis
PDB id:
3bin
Name: Cell adhesion
Title: Structure of the dal-1 and tslc1 (372-383) complex
Structure: Band 4.1-like protein 3. Chain: a. Fragment: ferm domain. Synonym: 4.1b, differentially expressed in adenocarcinoma of the lung protein 1, dal-1. Engineered: yes. Cell adhesion molecule 1. Chain: b. Fragment: peptide from cytoplasmic domain, unp residues 400-411.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: epb41l3, dal1, kiaa0987. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: peptide synthetic
Resolution:
2.30Å     R-factor:   0.181     R-free:   0.230
Authors: R.D.Busam,C.H.Arrowsmith,R.Collins,L.G.Dahlgren,A.M.Edwards,S.Flodin, A.Flores,S.Graslund,M.Hammarstrom,A.Johansson,I.Johansson,A.Kallas, T.Karlberg,T.Kotenyova,L.Lehtio,M.Moche,M.E.Nilsson,P.Nordlund, T.Nyman,J.Sagemark,L.Svensson,A.G.Thorsell,L.Tresaugues,S.Van Den Berg,J.Weigelt,M.Welin,H.Berglund,C.Persson,B.M.Hallberg
Key ref: R.D.Busam et al. (2011). Structural basis of tumor suppressor in lung cancer 1 (TSLC1) binding to differentially expressed in adenocarcinoma of the lung (DAL-1/4.1B). J Biol Chem, 286, 4511-4516. PubMed id: 21131357
Date:
30-Nov-07     Release date:   15-Jan-08    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9Y2J2  (E41L3_HUMAN) -  Band 4.1-like protein 3 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1087 a.a.
281 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
J Biol Chem 286:4511-4516 (2011)
PubMed id: 21131357  
 
 
Structural basis of tumor suppressor in lung cancer 1 (TSLC1) binding to differentially expressed in adenocarcinoma of the lung (DAL-1/4.1B).
R.D.Busam, A.G.Thorsell, A.Flores, M.Hammarström, C.Persson, B.Öbrink, B.M.Hallberg.
 
  ABSTRACT  
 
No abstract given.

 

 

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