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1B99

3'-FLUORO-URIDINE DIPHOSPHATE BINDING TO NUCLEOSIDE DIPHOSPHATE KINASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005840cellular_componentribosome
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0006183biological_processGTP biosynthetic process
A0006187biological_processdGTP biosynthetic process from dGDP
A0006228biological_processUTP biosynthetic process
A0006241biological_processCTP biosynthetic process
A0006414biological_processtranslational elongation
A0007186biological_processG protein-coupled receptor signaling pathway
A0009117biological_processnucleotide metabolic process
A0009142biological_processnucleoside triphosphate biosynthetic process
A0009617biological_processresponse to bacterium
A0015629cellular_componentactin cytoskeleton
A0016301molecular_functionkinase activity
A0019954biological_processasexual reproduction
A0030036biological_processactin cytoskeleton organization
A0030141cellular_componentsecretory granule
A0045335cellular_componentphagocytic vesicle
A0045920biological_processnegative regulation of exocytosis
A0046872molecular_functionmetal ion binding
A0048550biological_processnegative regulation of pinocytosis
A0050765biological_processnegative regulation of phagocytosis
B0004550molecular_functionnucleoside diphosphate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005840cellular_componentribosome
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0006183biological_processGTP biosynthetic process
B0006187biological_processdGTP biosynthetic process from dGDP
B0006228biological_processUTP biosynthetic process
B0006241biological_processCTP biosynthetic process
B0006414biological_processtranslational elongation
B0007186biological_processG protein-coupled receptor signaling pathway
B0009117biological_processnucleotide metabolic process
B0009142biological_processnucleoside triphosphate biosynthetic process
B0009617biological_processresponse to bacterium
B0015629cellular_componentactin cytoskeleton
B0016301molecular_functionkinase activity
B0019954biological_processasexual reproduction
B0030036biological_processactin cytoskeleton organization
B0030141cellular_componentsecretory granule
B0045335cellular_componentphagocytic vesicle
B0045920biological_processnegative regulation of exocytosis
B0046872molecular_functionmetal ion binding
B0048550biological_processnegative regulation of pinocytosis
B0050765biological_processnegative regulation of phagocytosis
C0004550molecular_functionnucleoside diphosphate kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005840cellular_componentribosome
C0005856cellular_componentcytoskeleton
C0005886cellular_componentplasma membrane
C0006183biological_processGTP biosynthetic process
C0006187biological_processdGTP biosynthetic process from dGDP
C0006228biological_processUTP biosynthetic process
C0006241biological_processCTP biosynthetic process
C0006414biological_processtranslational elongation
C0007186biological_processG protein-coupled receptor signaling pathway
C0009117biological_processnucleotide metabolic process
C0009142biological_processnucleoside triphosphate biosynthetic process
C0009617biological_processresponse to bacterium
C0015629cellular_componentactin cytoskeleton
C0016301molecular_functionkinase activity
C0019954biological_processasexual reproduction
C0030036biological_processactin cytoskeleton organization
C0030141cellular_componentsecretory granule
C0045335cellular_componentphagocytic vesicle
C0045920biological_processnegative regulation of exocytosis
C0046872molecular_functionmetal ion binding
C0048550biological_processnegative regulation of pinocytosis
C0050765biological_processnegative regulation of phagocytosis
D0004550molecular_functionnucleoside diphosphate kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005840cellular_componentribosome
D0005856cellular_componentcytoskeleton
D0005886cellular_componentplasma membrane
D0006183biological_processGTP biosynthetic process
D0006187biological_processdGTP biosynthetic process from dGDP
D0006228biological_processUTP biosynthetic process
D0006241biological_processCTP biosynthetic process
D0006414biological_processtranslational elongation
D0007186biological_processG protein-coupled receptor signaling pathway
D0009117biological_processnucleotide metabolic process
D0009142biological_processnucleoside triphosphate biosynthetic process
D0009617biological_processresponse to bacterium
D0015629cellular_componentactin cytoskeleton
D0016301molecular_functionkinase activity
D0019954biological_processasexual reproduction
D0030036biological_processactin cytoskeleton organization
D0030141cellular_componentsecretory granule
D0045335cellular_componentphagocytic vesicle
D0045920biological_processnegative regulation of exocytosis
D0046872molecular_functionmetal ion binding
D0048550biological_processnegative regulation of pinocytosis
D0050765biological_processnegative regulation of phagocytosis
E0004550molecular_functionnucleoside diphosphate kinase activity
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005840cellular_componentribosome
E0005856cellular_componentcytoskeleton
E0005886cellular_componentplasma membrane
E0006183biological_processGTP biosynthetic process
E0006187biological_processdGTP biosynthetic process from dGDP
E0006228biological_processUTP biosynthetic process
E0006241biological_processCTP biosynthetic process
E0006414biological_processtranslational elongation
E0007186biological_processG protein-coupled receptor signaling pathway
E0009117biological_processnucleotide metabolic process
E0009142biological_processnucleoside triphosphate biosynthetic process
E0009617biological_processresponse to bacterium
E0015629cellular_componentactin cytoskeleton
E0016301molecular_functionkinase activity
E0019954biological_processasexual reproduction
E0030036biological_processactin cytoskeleton organization
E0030141cellular_componentsecretory granule
E0045335cellular_componentphagocytic vesicle
E0045920biological_processnegative regulation of exocytosis
E0046872molecular_functionmetal ion binding
E0048550biological_processnegative regulation of pinocytosis
E0050765biological_processnegative regulation of phagocytosis
F0004550molecular_functionnucleoside diphosphate kinase activity
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0005840cellular_componentribosome
F0005856cellular_componentcytoskeleton
F0005886cellular_componentplasma membrane
F0006183biological_processGTP biosynthetic process
F0006187biological_processdGTP biosynthetic process from dGDP
F0006228biological_processUTP biosynthetic process
F0006241biological_processCTP biosynthetic process
F0006414biological_processtranslational elongation
F0007186biological_processG protein-coupled receptor signaling pathway
F0009117biological_processnucleotide metabolic process
F0009142biological_processnucleoside triphosphate biosynthetic process
F0009617biological_processresponse to bacterium
F0015629cellular_componentactin cytoskeleton
F0016301molecular_functionkinase activity
F0019954biological_processasexual reproduction
F0030036biological_processactin cytoskeleton organization
F0030141cellular_componentsecretory granule
F0045335cellular_componentphagocytic vesicle
F0045920biological_processnegative regulation of exocytosis
F0046872molecular_functionmetal ion binding
F0048550biological_processnegative regulation of pinocytosis
F0050765biological_processnegative regulation of phagocytosis
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE FUP A 160
ChainResidue
ALYS16
AHOH216
FHOH209
ATYR56
AHIS59
APHE64
AARG92
ATHR98
AARG109
AVAL116
AASN119

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE POP B 260
ChainResidue
BHIS59
BARG92
BHOH200
BHOH217

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE POP C 360
ChainResidue
CHIS59
CARG92
CTHR98
CARG109
CHOH218

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE POP D 460
ChainResidue
DHIS59
DARG92
DTHR98
DARG109
DHOH204
DHOH205

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE POP E 560
ChainResidue
EARG92
ETHR98
EARG109

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE POP F 660
ChainResidue
FHIS59
FARG92
FARG109
FASP125

Functional Information from PROSITE/UniProt
site_idPS00469
Number of Residues9
DetailsNDPK Nucleoside diphosphate kinase (NDPK) active site signature. NiiHGSDSV
ChainResidueDetails
AASN119-VAL127

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Pros-phosphohistidine intermediate
ChainResidueDetails
AHIS122
BHIS122
CHIS122
DHIS122
EHIS122
FHIS122

site_idSWS_FT_FI2
Number of Residues36
DetailsBINDING:
ChainResidueDetails
ALYS16
BTHR98
BARG109
BASN119
CLYS16
CPHE64
CARG92
CTHR98
CARG109
CASN119
DLYS16
APHE64
DPHE64
DARG92
DTHR98
DARG109
DASN119
ELYS16
EPHE64
EARG92
ETHR98
EARG109
AARG92
EASN119
FLYS16
FPHE64
FARG92
FTHR98
FARG109
FASN119
ATHR98
AARG109
AASN119
BLYS16
BPHE64
BARG92

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
AASN119
ALYS16

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
DTYR56
DLYS16

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
ETYR56
ELYS16

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
FTYR56
FLYS16

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
BASN119
BLYS16

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
CASN119
CLYS16

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
DASN119
DLYS16

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
EASN119
ELYS16

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
FASN119
FLYS16

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
ATYR56
ALYS16

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
BTYR56
BLYS16

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nsp
ChainResidueDetails
CTYR56
CLYS16

site_idMCSA1
Number of Residues5
DetailsM-CSA 150
ChainResidueDetails
ALYS16electrostatic stabiliser, hydrogen bond donor
ATYR56electrostatic stabiliser, hydrogen bond donor
AASN119electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, steric role
AHIS122hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
AGLU133hydrogen bond acceptor, increase nucleophilicity, steric role

site_idMCSA2
Number of Residues5
DetailsM-CSA 150
ChainResidueDetails
BLYS16electrostatic stabiliser, hydrogen bond donor
BTYR56electrostatic stabiliser, hydrogen bond donor
BASN119electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, steric role
BHIS122hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BGLU133hydrogen bond acceptor, increase nucleophilicity, steric role

site_idMCSA3
Number of Residues5
DetailsM-CSA 150
ChainResidueDetails
CLYS16electrostatic stabiliser, hydrogen bond donor
CTYR56electrostatic stabiliser, hydrogen bond donor
CASN119electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, steric role
CHIS122hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
CGLU133hydrogen bond acceptor, increase nucleophilicity, steric role

site_idMCSA4
Number of Residues5
DetailsM-CSA 150
ChainResidueDetails
DLYS16electrostatic stabiliser, hydrogen bond donor
DTYR56electrostatic stabiliser, hydrogen bond donor
DASN119electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, steric role
DHIS122hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
DGLU133hydrogen bond acceptor, increase nucleophilicity, steric role

site_idMCSA5
Number of Residues5
DetailsM-CSA 150
ChainResidueDetails
ELYS16electrostatic stabiliser, hydrogen bond donor
ETYR56electrostatic stabiliser, hydrogen bond donor
EASN119electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, steric role
EHIS122hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
EGLU133hydrogen bond acceptor, increase nucleophilicity, steric role

site_idMCSA6
Number of Residues5
DetailsM-CSA 150
ChainResidueDetails
FLYS16electrostatic stabiliser, hydrogen bond donor
FTYR56electrostatic stabiliser, hydrogen bond donor
FASN119electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, steric role
FHIS122hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
FGLU133hydrogen bond acceptor, increase nucleophilicity, steric role

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PDB entries from 2024-07-10

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