Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3EVW

Crystal structure of the Mimivirus NDK R107G mutant complexed with dTDP

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
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
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0004550molecular_functionnucleoside diphosphate kinase activity
C0005524molecular_functionATP binding
C0006183biological_processGTP biosynthetic process
C0006228biological_processUTP biosynthetic process
C0006241biological_processCTP biosynthetic process
C0009117biological_processnucleotide metabolic process
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0004550molecular_functionnucleoside diphosphate kinase activity
D0005524molecular_functionATP binding
D0006183biological_processGTP biosynthetic process
D0006228biological_processUTP biosynthetic process
D0006241biological_processCTP biosynthetic process
D0009117biological_processnucleotide metabolic process
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0046872molecular_functionmetal ion binding
E0000166molecular_functionnucleotide binding
E0004550molecular_functionnucleoside diphosphate kinase activity
E0005524molecular_functionATP binding
E0006183biological_processGTP biosynthetic process
E0006228biological_processUTP biosynthetic process
E0006241biological_processCTP biosynthetic process
E0009117biological_processnucleotide metabolic process
E0016301molecular_functionkinase activity
E0016740molecular_functiontransferase activity
E0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0004550molecular_functionnucleoside diphosphate kinase activity
F0005524molecular_functionATP binding
F0006183biological_processGTP biosynthetic process
F0006228biological_processUTP biosynthetic process
F0006241biological_processCTP biosynthetic process
F0009117biological_processnucleotide metabolic process
F0016301molecular_functionkinase activity
F0016740molecular_functiontransferase activity
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 160
ChainResidue
AARG86
ATYD138

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 161
ChainResidue
BARG86
BASP115
BTYD138

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 162
ChainResidue
CARG86
CASP115
CTYD138

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG D 163
ChainResidue
DASP115
DTYD138
DARG86

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG E 164
ChainResidue
EARG86
ETYD138

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG F 165
ChainResidue
FASP115
FTYD138

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TYD A 138
ChainResidue
ALYS9
ATYR50
AHIS53
ATYR58
AASN62
AARG86
AGLN89
AARG99
AILE106
AGLY107
AASN109
AMG160

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TYD B 138
ChainResidue
BLYS9
BHIS53
BTYR58
BASN62
BARG86
BARG99
BILE106
BGLY107
BASN109
BMG161

site_idAC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TYD C 138
ChainResidue
CLYS9
CTYR50
CHIS53
CTYR58
CASN62
CARG86
CGLN89
CARG99
CILE106
CGLY107
CASN109
CMG162

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TYD D 138
ChainResidue
DLYS9
DTYR50
DHIS53
DTYR58
DASN62
DARG86
DGLN89
DARG99
DILE106
DGLY107
DASN109
DMG163

site_idBC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TYD E 138
ChainResidue
ELYS9
ETYR50
EHIS53
ETYR58
EASN62
EARG86
EARG99
EILE106
EGLY107
EASN109
EMG164

site_idBC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TYD F 138
ChainResidue
FLYS9
FTYR50
FHIS53
FTYR58
FARG86
FGLN89
FARG99
FILE106
FGLY107
FASN109
FMG165

Functional Information from PROSITE/UniProt
site_idPS00469
Number of Residues9
DetailsNDPK Nucleoside diphosphate kinase (NDPK) active site signature. NliHASDSE
ChainResidueDetails
AASN109-GLU117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Pros-phosphohistidine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10030","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues30
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
AASN109
ALYS9

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
DTYR50
DLYS9

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
ETYR50
ELYS9

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
FTYR50
FLYS9

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
BASN109
BLYS9

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
CASN109
CLYS9

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
DASN109
DLYS9

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
EASN109
ELYS9

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
FASN109
FLYS9

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
ATYR50
ALYS9

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
BTYR50
BLYS9

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
CTYR50
CLYS9

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon