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7LUY

Crystal Structure of guanylate kinase from Bartonella henselae str. Houston-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004385molecular_functionguanylate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006163biological_processpurine nucleotide metabolic process
A0016301molecular_functionkinase activity
A0046037biological_processGMP metabolic process
A0046710biological_processGDP metabolic process
B0004385molecular_functionguanylate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006163biological_processpurine nucleotide metabolic process
B0016301molecular_functionkinase activity
B0046037biological_processGMP metabolic process
B0046710biological_processGDP metabolic process
C0004385molecular_functionguanylate kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006163biological_processpurine nucleotide metabolic process
C0016301molecular_functionkinase activity
C0046037biological_processGMP metabolic process
C0046710biological_processGDP metabolic process
D0004385molecular_functionguanylate kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006163biological_processpurine nucleotide metabolic process
D0016301molecular_functionkinase activity
D0046037biological_processGMP metabolic process
D0046710biological_processGDP metabolic process
E0004385molecular_functionguanylate kinase activity
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006163biological_processpurine nucleotide metabolic process
E0016301molecular_functionkinase activity
E0046037biological_processGMP metabolic process
E0046710biological_processGDP metabolic process
F0004385molecular_functionguanylate kinase activity
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006163biological_processpurine nucleotide metabolic process
F0016301molecular_functionkinase activity
F0046037biological_processGMP metabolic process
F0046710biological_processGDP metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 301
ChainResidue
AGLY29
AALA30
AGLY31
ALYS32
ASER33
AHOH424

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 302
ChainResidue
AHOH430
AHOH454
ALYS121
AHIS172
ASER175

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 303
ChainResidue
ALYS75
AARG78
BARG78
BTRP86

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 304
ChainResidue
AARG57
AHIS90
AARG162
AHOH414

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 B 301
ChainResidue
BLYS121
BHIS172
BSER175
BHOH426
BHOH438
BHOH459

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO B 302
ChainResidue
AARG78
ATRP86
BARG78

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO B 303
ChainResidue
BHIS90
BASN165

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 C 301
ChainResidue
CLYS121
CGLN171
CHIS172
CSER175

site_idAC9
Number of Residues6
Detailsbinding site for residue SO4 D 301
ChainResidue
DGLY29
DALA30
DGLY31
DLYS32
DSER33
DHOH405

site_idAD1
Number of Residues5
Detailsbinding site for residue SO4 D 302
ChainResidue
DLYS121
DHIS172
DARG174
DSER175
DHOH415

site_idAD2
Number of Residues3
Detailsbinding site for residue EDO D 303
ChainResidue
CASN214
DTRP173
DARG174

site_idAD3
Number of Residues1
Detailsbinding site for residue EDO D 304
ChainResidue
DLYS121

site_idAD4
Number of Residues7
Detailsbinding site for residue SO4 E 301
ChainResidue
EGLY29
EALA30
EGLY31
ELYS32
ESER33
EARG147
EARG151

site_idAD5
Number of Residues5
Detailsbinding site for residue SO4 E 302
ChainResidue
CARG76
ETYR117
EHIS172
ESER175
EHOH420

site_idAD6
Number of Residues3
Detailsbinding site for residue EDO E 303
ChainResidue
ETHR34
EARG147
EARG150

site_idAD7
Number of Residues3
Detailsbinding site for residue EDO E 304
ChainResidue
EASP154
ESER155
EGLN156

site_idAD8
Number of Residues4
Detailsbinding site for residue EDO E 305
ChainResidue
BASN214
EGLN171
ETRP173
EARG174

site_idAD9
Number of Residues5
Detailsbinding site for residue EDO E 306
ChainResidue
ETHR131
EASP177
EGLU199
ELYS202
EHOH408

site_idAE1
Number of Residues4
Detailsbinding site for residue SO4 F 301
ChainResidue
DARG76
FTYR117
FHIS172
FSER175

Functional Information from PROSITE/UniProt
site_idPS00856
Number of Residues18
DetailsGUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRqkRpsEvdGlhYhFI
ChainResidueDetails
ATHR52-ILE69

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00328
ChainResidueDetails
ASER26
BSER26
CSER26
DSER26
ESER26
FSER26

219869

PDB entries from 2024-05-15

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