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2HK7

Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with mercury at 2.5 angstrom resolution

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
B0004764molecular_functionshikimate 3-dehydrogenase (NADP+) activity
B0005829cellular_componentcytosol
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0009423biological_processchorismate biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0019632biological_processshikimate metabolic process
B0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 270
ChainResidue
AHIS18
AHOH321
AHOH322

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE HG A 271
ChainResidue
AMET1

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE HG A 272
ChainResidue
ACYS253

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE HG B 270
ChainResidue
BHIS18

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE HG B 271
ChainResidue
BMET1

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE HG B 272
ChainResidue
BCYS253

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000305|PubMed:17649975
ChainResidueDetails
ALYS70
BLYS70

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:17649975
ChainResidueDetails
ASER19
BSER19
BASP82
BASN91
BASP106
BGLY130
BILE214
BTYR216
BGLY235
BGLN242
AASP82
AASN91
AASP106
AGLY130
AILE214
ATYR216
AGLY235
AGLN242

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222
ChainResidueDetails
ATHR66
BTHR66

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000305|PubMed:17649975
ChainResidueDetails
AASN153
BASN153

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1nvt
ChainResidueDetails
AASN97

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1nvt
ChainResidueDetails
BASN97

223166

PDB entries from 2024-07-31

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