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PDBsum entry 4ba1

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
4ba1

 

 

 

 

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Contents
Protein chains
272 a.a.
234 a.a.
204 a.a.
Ligands
1PE
PEG
PO4 ×2
Metals
_NA
Waters ×445
PDB id:
4ba1
Name: Hydrolase
Title: Archaeal exosome (rrp4-rrp41(d182a)-rrp42) bound to inorganic phosphate
Structure: Probable exosome complex exonuclease 2. Chain: a. Synonym: rrp42. Engineered: yes. Probable exosome complex exonuclease 1. Chain: b. Synonym: rrp41. Engineered: yes. Mutation: yes.
Source: Sulfolobus solfataricus. Organism_taxid: 2287. Expressed in: escherichia coli. Expression_system_taxid: 83333.
Resolution:
1.80Å     R-factor:   0.186     R-free:   0.222
Authors: E.Lorentzen,E.Conti
Key ref: E.Lorentzen and E.Conti (2012). Crystal structure of a 9-subunit archaeal exosome in pre-catalytic states of the phosphorolytic reaction. Archaea, 2012, 721869. PubMed id: 23319881
Date:
10-Sep-12     Release date:   03-Oct-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9UXC0  (RRP42_SULSO) -  Exosome complex component Rrp42 from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Seq:
Struc:
275 a.a.
272 a.a.*
Protein chain
Pfam   ArchSchema ?
Q9UXC2  (RRP41_SULSO) -  Exosome complex component Rrp41 from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Seq:
Struc:
248 a.a.
234 a.a.*
Protein chain
Pfam   ArchSchema ?
Q9UXC4  (RRP4_SACS2) -  Exosome complex component Rrp4 from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Seq:
Struc:
249 a.a.
204 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain B: E.C.3.1.13.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Archaea 2012:721869 (2012)
PubMed id: 23319881  
 
 
Crystal structure of a 9-subunit archaeal exosome in pre-catalytic states of the phosphorolytic reaction.
E.Lorentzen, E.Conti.
 
  ABSTRACT  
 
No abstract given.

 

 

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