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2WU8

Structural studies of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv

Functional Information from GO Data
ChainGOidnamespacecontents
A0004347molecular_functionglucose-6-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
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
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1556
ChainResidue
ATHR212
ATHR215

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1557
ChainResidue
ASER180
AARG182
AHOH2093

Functional Information from PROSITE/UniProt
site_idPS00174
Number of Residues18
DetailsP_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GvVWgidsFDQwGVElgK
ChainResidueDetails
AGLY497-LYS514

site_idPS00765
Number of Residues14
DetailsP_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSVdSAIG
ChainResidueDetails
AASP267-GLY280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00473
ChainResidueDetails
AGLU357

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00473
ChainResidueDetails
AHIS388
ALYS514

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dqr
ChainResidueDetails
AARG272
ALYS514
ALYS211
AGLU357
AGLY271
AGLU217

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqr
ChainResidueDetails
AHIS388

226707

PDB entries from 2024-10-30

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