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PDBsum entry 4xck

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
4xck

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
306 a.a.
Ligands
RIB ×2
ADP ×5
Metals
_CS ×4
Waters ×248
PDB id:
4xck
Name: Transferase
Title: Vibrio cholerae o395 ribokinase complexed with adp, ribose and cesium ion.
Structure: Ribokinase. Chain: a, b, c, d. Engineered: yes
Source: Vibrio cholerae serotype o1 (strain atcc 39541 / classical ogawa 395 / o395). Organism_taxid: 345073. Strain: atcc 39541 / classical ogawa 395 / o395. Atcc: 39541. Gene: rbsk, vc0395_0007, vc395_a0124. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.37Å     R-factor:   0.191     R-free:   0.251
Authors: R.Paul,M.D.Patra,U.Sen
Key ref: R.Paul et al. (2015). Crystal structure of apo and ligand bound vibrio cholerae ribokinase (Vc-RK): role of monovalent cation induced activation and structural flexibility in sugar phosphorylation. Adv Exp Med Biol, 842, 293-307. PubMed id: 25408351 DOI: 10.1007/978-3-319-11280-0_19
Date:
18-Dec-14     Release date:   21-Jan-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
A0A0H2UL04  (A0A0H2UL04_VIBC3) -  Ribokinase from Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Seq:
Struc:
309 a.a.
306 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.1.15  - ribokinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: D-ribose + ATP = D-ribose 5-phosphate + ADP + H+
D-ribose
+
ATP
Bound ligand (Het Group name = RIB)
corresponds exactly
=
D-ribose 5-phosphate
Bound ligand (Het Group name = ADP)
corresponds exactly
+ ADP
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1007/978-3-319-11280-0_19 Adv Exp Med Biol 842:293-307 (2015)
PubMed id: 25408351  
 
 
Crystal structure of apo and ligand bound vibrio cholerae ribokinase (Vc-RK): role of monovalent cation induced activation and structural flexibility in sugar phosphorylation.
R.Paul, M.D.Patra, U.Sen.
 
  ABSTRACT  
 
No abstract given.

 

 

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