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3FF1

Structure of Glucose 6-phosphate Isomerase from Staphylococcus aureus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004347molecular_functionglucose-6-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0048029molecular_functionmonosaccharide binding
A0051156biological_processglucose 6-phosphate metabolic process
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
B0004347molecular_functionglucose-6-phosphate isomerase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0048029molecular_functionmonosaccharide binding
B0051156biological_processglucose 6-phosphate metabolic process
B0097367molecular_functioncarbohydrate derivative binding
B1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE G6Q B 444
ChainResidue
AGLU104
BHOH724
BHOH780
BHOH1196
BHOH1356
BLYS70
BGLU71
BSER73
BASP74
BASN103
BGLU104
BHOH453
BHOH713

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 445
ChainResidue
AASN101
AHOH1298
BGLU104
BTYR105
BHOH750
BHOH878

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 446
ChainResidue
AHOH1197
BSER60
BHOH452
BHOH565
BHOH1198

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 444
ChainResidue
ALYS70
ASER73
AHOH1076
AHOH1193
AHOH1194
AHOH1195

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 447
ChainResidue
AHOH1402
BASN327
BHOH771
BHOH787
BHOH978
BHOH980

Functional Information from PROSITE/UniProt
site_idPS00174
Number of Residues18
DetailsP_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GyQLgvnpFNQpGVEayK
ChainResidueDetails
AGLY403-LYS420

site_idPS00765
Number of Residues14
DetailsP_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DdVGGRYSVlTAVG
ChainResidueDetails
AASP197-GLY210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00473
ChainResidueDetails
AGLU285
BGLU285

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00473
ChainResidueDetails
AHIS306
ALYS420
BHIS306
BLYS420

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dqr
ChainResidueDetails
AGLY201
AGLU145
AGLU285
ALYS139
ALYS420
AARG202

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dqr
ChainResidueDetails
BGLY201
BGLU145
BGLU285
BLYS139
BLYS420
BARG202

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqr
ChainResidueDetails
AHIS306

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqr
ChainResidueDetails
BHIS306

site_idCSA5
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dqr
ChainResidueDetails
AGLY201
AGLU145
AGLU285
ALYS429
ALYS139
AARG202

site_idCSA6
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dqr
ChainResidueDetails
BGLY201
BGLU145
BGLU285
BLYS429
BLYS139
BARG202

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PDB entries from 2024-05-01

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