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3UJH

Crystal structure of substrate-bound Glucose-6-phosphate isomerase from Toxoplasma gondii

Functional Information from GO Data
ChainGOidnamespacecontents
A0004347molecular_functionglucose-6-phosphate isomerase activity
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
B0004347molecular_functionglucose-6-phosphate isomerase activity
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0097367molecular_functioncarbohydrate derivative binding
B1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 565
ChainResidue
AMET325
ATYR494
AARG497

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 565
ChainResidue
BGLN489
BTHR44
BASP45
BGLN46
BVAL48
BMET308
BHIS311

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 566
ChainResidue
BVAL134
BARG135
BLEU147
BVAL148
BARG182
BLEU291
BHOH591

Functional Information from PROSITE/UniProt
site_idPS00174
Number of Residues18
DetailsP_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GwLWginsFDQwGVElgK
ChainResidueDetails
AGLY502-LYS519

site_idPS00765
Number of Residues14
DetailsP_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSVtSAVG
ChainResidueDetails
AASP272-GLY285

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PDB entries from 2024-07-24

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