Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3FBF

Crystal structure of the Mimivirus NDK N62L 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
A0009142biological_processnucleoside triphosphate biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
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
B0016310biological_processphosphorylation
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
C0009142biological_processnucleoside triphosphate biosynthetic process
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
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
D0009142biological_processnucleoside triphosphate biosynthetic process
D0016301molecular_functionkinase activity
D0016310biological_processphosphorylation
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
E0009142biological_processnucleoside triphosphate biosynthetic process
E0016301molecular_functionkinase activity
E0016310biological_processphosphorylation
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
F0009142biological_processnucleoside triphosphate biosynthetic process
F0016301molecular_functionkinase activity
F0016310biological_processphosphorylation
F0016740molecular_functiontransferase activity
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 160
ChainResidue
AARG86
ATYD138
AHOH167

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TYD A 138
ChainResidue
AARG99
AILE106
AARG107
AASN109
AMG160
AHOH167
ALYS9
AHIS53
ATYR58
ALEU62
AARG86
AGLN89

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 161
ChainResidue
BTYD138

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TYD B 138
ChainResidue
BLYS9
BTYR50
BHIS53
BTYR58
BLEU62
BARG99
BILE106
BARG107
BASN109
BMG161

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 162
ChainResidue
CARG86
CASP115
CTYD138

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TYD C 138
ChainResidue
CLYS9
CHIS53
CTYR58
CLEU62
CARG86
CARG99
CILE106
CARG107
CASN109
CHOH155
CMG162

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG D 163
ChainResidue
DASP115
DTYD138

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TYD D 138
ChainResidue
DLYS9
DHIS53
DTYR58
DLEU62
DARG86
DGLN89
DARG99
DILE106
DARG107
DASN109
DMG163

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG E 164
ChainResidue
ETYD138

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TYD E 138
ChainResidue
ELYS9
EHIS53
ETYR58
ELEU62
EARG86
EARG99
EILE106
EARG107
EASN109
EHOH160
EMG164

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG F 165
ChainResidue
FARG86
FASP115
FTYD138

site_idBC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TYD F 138
ChainResidue
FLYS9
FHIS53
FTYR58
FLEU62
FARG86
FGLN89
FARG99
FILE106
FARG107
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
DetailsACT_SITE: Pros-phosphohistidine intermediate => ECO:0000255|PROSITE-ProRule:PRU10030
ChainResidueDetails
AHIS112
BHIS112
CHIS112
DHIS112
EHIS112
FHIS112

site_idSWS_FT_FI2
Number of Residues30
DetailsBINDING:
ChainResidueDetails
ALYS9
BASN109
CLYS9
CTYR58
CARG86
CARG99
CASN109
DLYS9
DTYR58
DARG86
DARG99
ATYR58
DASN109
ELYS9
ETYR58
EARG86
EARG99
EASN109
FLYS9
FTYR58
FARG86
FARG99
AARG86
FASN109
AARG99
AASN109
BLYS9
BTYR58
BARG86
BARG99

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon