3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.71
BRENDA Enzyme Link: BRENDA 2.7.1.71
KEGG Enzyme Link: KEGG2.7.1.71
BioCyc Enzyme Link: BioCyc 2.7.1.71
ExPASy Enzyme Link: ExPASy2.7.1.71
EC2PDB Enzyme Link: EC2PDB 2.7.1.71
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.71
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.71
IntEnz Enzyme Link: IntEnz 2.7.1.71
MEDLINE Enzyme Link: MEDLINE 2.7.1.71
MSA:

2.7.1.71;

Phylogenetic Tree:

2.7.1.71;

Uniprot:
M-CSA:
RHEA:13121 ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The role of the C8 proton of ATP in the catalysis of shikimate kinase and adenylate kinase.Kenyon CP, Roth RL2012 Aug 1022876783
Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine.Krell T, Maclean J, Boam DJ, Cooper A, Resmini M, Brocklehurst K, Kelly SM, Price NC, Lapthorn AJ, Coggins JR2001 Jun11369852
Archaeal shikimate kinase, a new member of the GHMP-kinase family.Daugherty M, Vonstein V, Overbeek R, Osterman A2001 Jan11114929