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2F3T

Crystal Structure Of E.coli Guanylate Kinase In Complex With Ganciclovir monophosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004385molecular_functionGMP kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006163biological_processpurine nucleotide metabolic process
A0009179biological_processpurine ribonucleoside diphosphate metabolic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0042802molecular_functionidentical protein binding
A0046037biological_processGMP metabolic process
A0046710biological_processGDP metabolic process
B0000166molecular_functionnucleotide binding
B0004385molecular_functionGMP kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006163biological_processpurine nucleotide metabolic process
B0009179biological_processpurine ribonucleoside diphosphate metabolic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0042802molecular_functionidentical protein binding
B0046037biological_processGMP metabolic process
B0046710biological_processGDP metabolic process
C0000166molecular_functionnucleotide binding
C0004385molecular_functionGMP kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006163biological_processpurine nucleotide metabolic process
C0009179biological_processpurine ribonucleoside diphosphate metabolic process
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0042802molecular_functionidentical protein binding
C0046037biological_processGMP metabolic process
C0046710biological_processGDP metabolic process
D0000166molecular_functionnucleotide binding
D0004385molecular_functionGMP kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006163biological_processpurine nucleotide metabolic process
D0009179biological_processpurine ribonucleoside diphosphate metabolic process
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0042802molecular_functionidentical protein binding
D0046037biological_processGMP metabolic process
D0046710biological_processGDP metabolic process
E0000166molecular_functionnucleotide binding
E0004385molecular_functionGMP kinase activity
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006163biological_processpurine nucleotide metabolic process
E0009179biological_processpurine ribonucleoside diphosphate metabolic process
E0016301molecular_functionkinase activity
E0016740molecular_functiontransferase activity
E0042802molecular_functionidentical protein binding
E0046037biological_processGMP metabolic process
E0046710biological_processGDP metabolic process
F0000166molecular_functionnucleotide binding
F0004385molecular_functionGMP kinase activity
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006163biological_processpurine nucleotide metabolic process
F0009179biological_processpurine ribonucleoside diphosphate metabolic process
F0016301molecular_functionkinase activity
F0016740molecular_functiontransferase activity
F0042802molecular_functionidentical protein binding
F0046037biological_processGMP metabolic process
F0046710biological_processGDP metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE LGP A 300
ChainResidue
ASER38
AARG42
AARG45
ATYR54
AGLU73
ATYR82
ATHR84

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LGP A 301
ChainResidue
BARG45
BTYR54
BGLU73
BALA75
BVAL77
BTYR82
BTHR84
BSER38
BARG42

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LGP A 302
ChainResidue
ESER38
EARG42
EARG45
ETYR54
EGLU73
ETYR82

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE LGP A 303
ChainResidue
FSER38
FARG45
FTYR54
FGLU73
FTYR82
FHOH210
FHOH211

Functional Information from PROSITE/UniProt
site_idPS00856
Number of Residues18
DetailsGUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRqpRpgEvhGehYfFV
ChainResidueDetails
ATHR40-VAL57

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AALA11
BALA11
CALA11
DALA11
EALA11
FALA11

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PDB entries from 2025-06-25

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