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PDBsum entry 4u3j

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protein ligands metals Protein-protein interface(s) links
Structural protein/protein binding PDB id
4u3j

 

 

 

 

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Contents
Protein chains
431 a.a.
417 a.a.
241 a.a.
Ligands
GTP ×2
Metals
_MG ×2
Waters ×21
PDB id:
4u3j
Name: Structural protein/protein binding
Title: Tog2:alpha/beta-tubulin complex
Structure: Tubulin alpha-1 chain. Chain: a. Engineered: yes. Tubulin beta chain. Chain: b. Synonym: beta-tubulin. Engineered: yes. Mutation: yes. Protein stu2.
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: tub1. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932. Gene: tub2. Gene: stu2. Expressed in: escherichia coli.
Resolution:
2.81Å     R-factor:   0.220     R-free:   0.259
Authors: P.Ayaz,L.M.Rice
Key ref: P.Ayaz et al. (2014). A tethered delivery mechanism explains the catalytic action of a microtubule polymerase. Elife, 3, e03069. PubMed id: 25097237 DOI: 10.7554/eLife.03069
Date:
22-Jul-14     Release date:   20-Aug-14    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P09733  (TBA1_YEAST) -  Tubulin alpha-1 chain from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
447 a.a.
431 a.a.
Protein chain
Pfam   ArchSchema ?
P02557  (TBB_YEAST) -  Tubulin beta chain from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
457 a.a.
417 a.a.*
Protein chain
Pfam   ArchSchema ?
P46675  (STU2_YEAST) -  Protein STU2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
888 a.a.
241 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.3.6.5.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.7554/eLife.03069 Elife 3:e03069 (2014)
PubMed id: 25097237  
 
 
A tethered delivery mechanism explains the catalytic action of a microtubule polymerase.
P.Ayaz, S.Munyoki, E.A.Geyer, F.A.Piedra, E.S.Vu, R.Bromberg, Z.Otwinowski, N.V.Grishin, C.A.Brautigam, L.M.Rice.
 
  ABSTRACT  
 
No abstract given.

 

 

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