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1Z6G

Crystal structure of guanylate kinase from Plasmodium falciparum

Functional Information from GO Data
ChainGOidnamespacecontents
A0004385molecular_functionguanylate kinase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006163biological_processpurine nucleotide metabolic process
A0006186biological_processobsolete dGDP phosphorylation
A0016301molecular_functionkinase activity
A0046037biological_processGMP metabolic process
A0046710biological_processGDP metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 400
ChainResidue
ASER13
AGLY14
AVAL15
AGLY16
ALYS17
AGLY18
AGLU101

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AASN79
AHOH604
AARG41
ALYS42

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
ALYS43
ALYS48
AGLU49
AHOH522
AHOH586

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
ASER13
ATYR76
ALEU136
AARG139
AASN140
AHOH616

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
AARG135

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE EPE A 430
ChainResidue
APRO12
ASER13
AASP74
AASN75
AASN103
AASN105
AGLN153
ALEU154
AGLU157
AHOH507
AHOH635

Functional Information from PROSITE/UniProt
site_idPS00856
Number of Residues18
DetailsGUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRkkRekEkeGvdYyFI
ChainResidueDetails
ATHR39-ILE56

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PDB entries from 2024-11-06

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