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4WIN

Crystal structure of the GATase domain from Plasmodium falciparum GMP synthetase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003922molecular_functionGMP synthase (glutamine-hydrolyzing) activity
A0005524molecular_functionATP binding
A0006177biological_processGMP biosynthetic process
B0003922molecular_functionGMP synthase (glutamine-hydrolyzing) activity
B0005524molecular_functionATP binding
B0006177biological_processGMP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue NO3 A 1001
ChainResidue
AASN13
APHE19
ATHR35
BASN13
BPHE19
BTHR35
BLYS36
BASP37

site_idAC2
Number of Residues7
Detailsbinding site for residue NO3 A 1002
ChainResidue
AGLN17
ATYR18
AGLY57
AGLY58
AHIS208
BTYR60
ASER16

site_idAC3
Number of Residues5
Detailsbinding site for residue NO3 B 301
ChainResidue
ATYR60
BSER16
BGLN17
BGLY58
BHIS208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile; for GATase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU00605","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21413787","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26592566","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"For GATase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU00605","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26592566","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WIO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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