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8PB9

Cryo-EM structure of the c-di-GMP-bound FleQ-FleN master regulator complex from Pseudomonas aeruginosa

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0009898cellular_componentcytoplasmic side of plasma membrane
A0016887molecular_functionATP hydrolysis activity
A0051782biological_processnegative regulation of cell division
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0009898cellular_componentcytoplasmic side of plasma membrane
B0016887molecular_functionATP hydrolysis activity
B0051782biological_processnegative regulation of cell division
C0005524molecular_functionATP binding
C0006355biological_processregulation of DNA-templated transcription
C0008134molecular_functiontranscription factor binding
C0016887molecular_functionATP hydrolysis activity
D0005524molecular_functionATP binding
D0006355biological_processregulation of DNA-templated transcription
D0008134molecular_functiontranscription factor binding
D0016887molecular_functionATP hydrolysis activity
E0005524molecular_functionATP binding
E0006355biological_processregulation of DNA-templated transcription
E0008134molecular_functiontranscription factor binding
E0016887molecular_functionATP hydrolysis activity
Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VLIlGESGTGKevV
ChainResidueDetails
DVAL170-VAL183

site_idPS00676
Number of Residues16
DetailsSIGMA54_INTERACT_2 Sigma-54 interaction domain ATP-binding region B signature. GrFelANGGTLFLDEI
ChainResidueDetails
DGLY232-ILE247

site_idPS00688
Number of Residues10
DetailsSIGMA54_INTERACT_3 Sigma-54 interaction domain C-terminal part signature. WPGNVRELaN
ChainResidueDetails
DTRP358-ASN367

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000305|PubMed:28065505, ECO:0007744|PDB:5J1J
ChainResidueDetails
ALYS19
BARG221
AGLU153
AASN181
APRO215
AARG221
BLYS19
BGLU153
BASN181
BPRO215

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:26712005, ECO:0007744|PDB:5EXT
ChainResidueDetails
DVAL147
EGLY177
EARG334
EARG363
DGLY177
DARG334
DARG363
CVAL147
CGLY177
CARG334
CARG363
EVAL147

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PDB entries from 2024-09-11

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