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PDBsum entry 4z7c

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protein ligands metals links
Lyase PDB id
4z7c

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
324 a.a.
Ligands
PO4 ×2
GOL
Metals
_NA
Waters ×140
PDB id:
4z7c
Name: Lyase
Title: Diphosphomevalonate decarboxylase from the sulfolobus solfataricus, space group h32
Structure: Diphosphomevalonate decarboxylase. Chain: a. Fragment: unp residues 2-325. Synonym: dmd. Engineered: yes
Source: Sulfolobus solfataricus (strain atcc 35092 / dsm 1617 / jcm 11322 / p2). Organism_taxid: 273057. Strain: atcc 35092 / dsm 1617 / jcm 11322 / p2. Gene: sso2989. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.212     R-free:   0.237
Authors: H.Unno,A.Hattori,H.Hemmi
Key ref: A.Hattori et al. (2015). In Vivo Formation of the Protein Disulfide Bond That Enhances the Thermostability of Diphosphomevalonate Decarboxylase, an Intracellular Enzyme from the Hyperthermophilic Archaeon Sulfolobus solfataricus. J Bacteriol, 197, 3463-3471. PubMed id: 26303832 DOI: 10.1128/JB.00352-15
Date:
07-Apr-15     Release date:   16-Sep-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q97UL5  (DMD_SULSO) -  Diphosphomevalonate decarboxylase from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Seq:
Struc:
325 a.a.
324 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.1.1.33  - diphosphomevalonate decarboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Terpenoid biosynthesis
      Reaction: (R)-5-diphosphomevalonate + ATP = isopentenyl diphosphate + ADP + phosphate + CO2
(R)-5-diphosphomevalonate
+ ATP
= isopentenyl diphosphate
+ ADP
+ phosphate
+
CO2
Bound ligand (Het Group name = PO4)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1128/JB.00352-15 J Bacteriol 197:3463-3471 (2015)
PubMed id: 26303832  
 
 
In Vivo Formation of the Protein Disulfide Bond That Enhances the Thermostability of Diphosphomevalonate Decarboxylase, an Intracellular Enzyme from the Hyperthermophilic Archaeon Sulfolobus solfataricus.
A.Hattori, H.Unno, S.Goda, K.Motoyama, T.Yoshimura, H.Hemmi.
 
  ABSTRACT  
 
No abstract given.

 

 

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