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PDBsum entry 5ikc

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protein metals Protein-protein interface(s) links
Transferase PDB id
5ikc

 

 

 

 

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Contents
Protein chains
213 a.a.
211 a.a.
89 a.a.
Metals
_CL ×2
Waters ×385
PDB id:
5ikc
Name: Transferase
Title: X-ray structure of the n-terminal domain of human doublecortin in complex with fab
Structure: Mab 6h10 light chain. Chain: a, l. Engineered: yes. Ighg protein. Chain: b, h. Engineered: yes. Neuronal migration protein doublecortin. Chain: m, n. Fragment: n-terminal domain, unp residues 133-221.
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: lc. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ighg. Homo sapiens. Human.
Resolution:
2.06Å     R-factor:   0.201     R-free:   0.265
Authors: A.Ruf,M.Stihle,J.Benz,R.Thoma,M.G.Rudolph
Key ref: D.Burger et al. (2016). Crystal Structures of the Human Doublecortin C- and N-terminal Domains in Complex with Specific Antibodies. J Biol Chem, 291, 16292-16306. PubMed id: 27226599 DOI: 10.1074/jbc.M116.726547
Date:
03-Mar-16     Release date:   18-May-16    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
A0A0U5BC76  (A0A0U5BC76_MOUSE) -  MAb 6H10 light chain from Mus musculus
Seq:
Struc:
234 a.a.
213 a.a.*
Protein chains
Pfam   ArchSchema ?
Q569X1  (Q569X1_MOUSE) -  Ighg protein from Mus musculus
Seq:
Struc:
476 a.a.
211 a.a.*
Protein chains
Pfam   ArchSchema ?
O43602  (DCX_HUMAN) -  Neuronal migration protein doublecortin from Homo sapiens
Seq:
Struc:
365 a.a.
89 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 57 residue positions (black crosses)

 

 
DOI no: 10.1074/jbc.M116.726547 J Biol Chem 291:16292-16306 (2016)
PubMed id: 27226599  
 
 
Crystal Structures of the Human Doublecortin C- and N-terminal Domains in Complex with Specific Antibodies.
D.Burger, M.Stihle, A.Sharma, P.Di Lello, J.Benz, B.D'Arcy, M.Debulpaep, D.Fry, W.Huber, T.Kremer, T.Laeremans, H.Matile, A.Ross, A.C.Rufer, G.Schoch, M.O.Steinmetz, J.Steyaert, M.G.Rudolph, R.Thoma, A.Ruf.
 
  ABSTRACT  
 
No abstract given.

 

 

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