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3MPD

Crystal structure of nucleoside diphosphate kinase from encephalitozoon cuniculi, cubic form, apo

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005524molecular_functionATP binding
A0006183biological_processGTP biosynthetic process
A0006228biological_processUTP biosynthetic process
A0006241biological_processCTP biosynthetic process
A0009117biological_processnucleotide metabolic process
A0009142biological_processnucleoside triphosphate biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0004550molecular_functionnucleoside diphosphate kinase activity
B0005524molecular_functionATP binding
B0006183biological_processGTP biosynthetic process
B0006228biological_processUTP biosynthetic process
B0006241biological_processCTP biosynthetic process
B0009117biological_processnucleotide metabolic process
B0009142biological_processnucleoside triphosphate biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 148
ChainResidue
APHE141
AASP142
ALYS143
AGLU144
AHOH243

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Pros-phosphohistidine intermediate => ECO:0000250
ChainResidueDetails
AHIS115
BHIS115

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS9
BASN112
AARG85
ATHR91
AARG102
AASN112
BLYS9
BARG85
BTHR91
BARG102

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PDB entries from 2025-06-18

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