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PDBsum entry 2xrp

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protein ligands Protein-protein interface(s) links
Structural protein PDB id
2xrp

 

 

 

 

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Contents
Protein chains
426 a.a. *
429 a.a. *
95 a.a. *
Ligands
GDP ×4
GTP ×4
* Residue conservation analysis
PDB id:
2xrp
Name: Structural protein
Title: Human doublecortin n-dc repeat (1mjd) and mammalian tubulin (1jff and 3hke) docked into the 8-angstrom cryo-em map of doublecortin- stabilised microtubules
Structure: Tubulin beta-2b chain. Chain: a, c, e, g. Synonym: tubulin beta chain. Tubulin alpha-1d chain. Chain: b, d, f, h. Synonym: tubulin alpha chain. Neuronal migration protein doublecortin. Chain: i. Fragment: residues 46-140.
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: brain. Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
Authors: F.J.Fourniol,C.V.Sindelar,B.Amigues,D.K.Clare,G.Thomas,M.Perderiset, F.Francis,A.Houdusse,C.A.Moores
Key ref: F.J.Fourniol et al. (2010). Template-free 13-protofilament microtubule-MAP assembly visualized at 8 A resolution. J Cell Biol, 191, 463-470. PubMed id: 20974813
Date:
18-Sep-10     Release date:   24-Nov-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q6B856  (TBB2B_BOVIN) -  Tubulin beta-2B chain from Bos taurus
Seq:
Struc:
445 a.a.
426 a.a.*
Protein chains
Pfam   ArchSchema ?
Q2HJ86  (TBA1D_BOVIN) -  Tubulin alpha-1D chain from Bos taurus
Seq:
Struc:
452 a.a.
429 a.a.*
Protein chain
Pfam   ArchSchema ?
O43602  (DCX_HUMAN) -  Neuronal migration protein doublecortin from Homo sapiens
Seq:
Struc:
365 a.a.
95 a.a.
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 11 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: Chains A, C, E, G: E.C.3.6.5.6  - tubulin GTPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: GTP + H2O = GDP + phosphate + H+
GTP
Bound ligand (Het Group name = GTP)
corresponds exactly
+ H2O
=
GDP
Bound ligand (Het Group name = GDP)
corresponds exactly
+ phosphate
+ H(+)
   Enzyme class 2: Chains B, D, F, H: E.C.3.6.5.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: Chain I: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
J Cell Biol 191:463-470 (2010)
PubMed id: 20974813  
 
 
Template-free 13-protofilament microtubule-MAP assembly visualized at 8 A resolution.
F.J.Fourniol, C.V.Sindelar, B.Amigues, D.K.Clare, G.Thomas, M.Perderiset, F.Francis, A.Houdusse, C.A.Moores.
 
  ABSTRACT  
 
No abstract given.

 

 

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