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4WIO

Crystal structure of the C89A GMP synthetase inactive mutant from Plasmodium falciparum in complex with glutamine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003921molecular_functionGMP synthase activity
A0003922molecular_functionGMP synthase (glutamine-hydrolyzing) activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006541biological_processglutamine metabolic process
A0016874molecular_functionligase activity
A0046037biological_processGMP metabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue GLN A 601
ChainResidue
AGLY58
AHIS208
ATYR60
AALA89
ATYR90
AGLN93
AASN169
AHIS170
AASN171
AASP172

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile; for GATase activity => ECO:0000255|PROSITE-ProRule:PRU00605, ECO:0000305|PubMed:21413787, ECO:0000305|PubMed:26592566
ChainResidueDetails
AALA89

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: For GATase activity => ECO:0000255|PROSITE-ProRule:PRU00605
ChainResidueDetails
AHIS208
AGLU210

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:26592566, ECO:0007744|PDB:4WIO
ChainResidueDetails
AGLN93
AASN169
AASP172
AHIS208

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00886
ChainResidueDetails
ASER262

site_idSWS_FT_FI5
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|Ref.6, ECO:0007744|PDB:3UOW
ChainResidueDetails
AARG336
AGLN476
ALYS547
AILE552
AGLU553

site_idSWS_FT_FI6
Number of Residues3
DetailsSITE: Important for ATPPase activity => ECO:0000269|PubMed:32358899
ChainResidueDetails
AASP371
AHIS388
AHIS389

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PDB entries from 2024-10-30

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