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1S4Q

Crystal Structure of Guanylate Kinase from Mycobacterium tuberculosis (Rv1389)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004017molecular_functionadenylate kinase activity
A0004385molecular_functionguanylate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006163biological_processpurine nucleotide metabolic process
A0016301molecular_functionkinase activity
A0019002molecular_functionGMP binding
A0019003molecular_functionGDP binding
A0046037biological_processGMP metabolic process
A0046710biological_processGDP metabolic process
A0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 300
ChainResidue
AASP179

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 301
ChainResidue
AALA31
AVAL32
AGLY33
ALYS34
ASER35

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT A 302
ChainResidue
APHE50
AGLN146
AGLN149
AALA150
AHOH353
AARG42
ALEU48
AHIS49

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 303
ChainResidue
AHIS93
AASP161
AARG165
AASP168

Functional Information from PROSITE/UniProt
site_idPS00856
Number of Residues18
DetailsGUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRapRpgEvdGvdYhFI
ChainResidueDetails
ATHR55-ILE72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY28

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:21969609
ChainResidueDetails
ASER2

219869

PDB entries from 2024-05-15

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