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8QST

Cryo-EM structure of the glucose-specific PTS transporter IICB from E. coli in the inward- and outward-facing conformation

Functional Information from PROSITE/UniProt
site_idPS01035
Number of Residues18
DetailsPTS_EIIB_TYPE_1_CYS PTS EIIB domains cysteine phosphorylation site signature. NItnldaCiTRLrVsVaD
ChainResidueDetails
AASN414-ASP431

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues166
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-LYS14
BGLU301-PRO309
ATHR72-ALA79
AASN133-ARG151
AHIS212-LYS249
AGLU301-PRO309
BMET1-LYS14
BTHR72-ALA79
BASN133-ARG151
BHIS212-LYS249

site_idSWS_FT_FI2
Number of Residues400
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU00426
ChainResidueDetails
ASER15-ALA35
ALEU356-ILE376
BSER15-ALA35
BALA51-PHE71
BLEU80-VAL100
BHIS112-PHE132
BPHE152-TRP172
BPRO191-HIS211
BLEU250-HIS270
BVAL280-ILE300
BILE310-GLY330
AALA51-PHE71
BLEU356-ILE376
ALEU80-VAL100
AHIS112-PHE132
APHE152-TRP172
APRO191-HIS211
ALEU250-HIS270
AVAL280-ILE300
AILE310-GLY330

site_idSWS_FT_FI3
Number of Residues146
DetailsTOPO_DOM: Periplasmic => ECO:0000255
ChainResidueDetails
AASN36-GLU50
BMET331-TRP355
ALEU101-LYS111
APRO173-ASN190
ASER271-LYS279
AMET331-TRP355
BASN36-GLU50
BLEU101-LYS111
BPRO173-ASN190
BSER271-LYS279

site_idSWS_FT_FI4
Number of Residues200
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:15919996
ChainResidueDetails
ALYS377-HIS477
BLYS377-HIS477

site_idSWS_FT_FI5
Number of Residues2
DetailsACT_SITE: Phosphocysteine intermediate; for EIIB activity => ECO:0000255|PROSITE-ProRule:PRU00421, ECO:0000305|PubMed:12716891, ECO:0000305|PubMed:18319344, ECO:0000305|PubMed:3129430
ChainResidueDetails
ACYS421
BCYS421

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphocysteine => ECO:0000269|PubMed:8505292
ChainResidueDetails
ACYS421
BCYS421

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PDB entries from 2024-09-25

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