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4FOS

Crystal Structure of Shikimate Dehydrogenase (aroE) Q237A Mutant from Helicobacter pylori in Complex with Shikimate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004764molecular_functionshikimate 3-dehydrogenase (NADP+) activity
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0019632biological_processshikimate metabolic process
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SKM A 500
ChainResidue
ASER16
AHOH623
AHOH627
ASER18
AASN63
AVAL64
ATHR65
ALYS69
AASN90
AASP105
ATYR210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000305|Ref.2, ECO:0000305|Ref.3
ChainResidueDetails
ALYS69

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|Ref.2, ECO:0000269|Ref.3, ECO:0000269|Ref.4
ChainResidueDetails
ATHR65
AALA237
ASER16

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|Ref.2, ECO:0000269|Ref.3
ChainResidueDetails
AASN90
AASP105

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|Ref.2
ChainResidueDetails
AGLY230
AGLY125

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|Ref.2
ChainResidueDetails
ASER181

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222
ChainResidueDetails
ALEU208

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|Ref.2, ECO:0000269|Ref.4
ChainResidueDetails
ATYR210

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PDB entries from 2024-06-12

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