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6J7E

Crystal Structure of Central domain of FleQ in complex with ATPgS and Mg

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006355biological_processregulation of DNA-templated transcription
A0008134molecular_functiontranscription factor binding
A0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues24
Detailsbinding site for residue AGS A 401
ChainResidue
AARG144
AGLU181
AVAL182
ALEU327
AARG334
AVAL362
AARG363
AMG402
AHOH504
AHOH508
AHOH514
ASER145
AHOH515
AHOH518
AHOH532
AHOH534
AHOH546
ALEU146
AVAL147
ASER176
AGLY177
ATHR178
AGLY179
ALYS180

site_idAC2
Number of Residues7
Detailsbinding site for residue MG A 402
ChainResidue
AGLU181
AASP245
AAGS401
AHOH504
AHOH508
AHOH518
AHOH534

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 403
ChainResidue
ASER176
AHIS287
AGLU301
AHOH502

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VLIlGESGTGKevV
ChainResidueDetails
AVAL170-VAL183

site_idPS00676
Number of Residues16
DetailsSIGMA54_INTERACT_2 Sigma-54 interaction domain ATP-binding region B signature. GrFelANGGTLFLDEI
ChainResidueDetails
AGLY232-ILE247

site_idPS00688
Number of Residues10
DetailsSIGMA54_INTERACT_3 Sigma-54 interaction domain C-terminal part signature. WPGNVRELaN
ChainResidueDetails
ATRP358-ASN367

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:26712005, ECO:0007744|PDB:5EXX
ChainResidueDetails
ALEU142
AASN186
AGLU330

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:26712005, ECO:0007744|PDB:5EXT
ChainResidueDetails
AVAL147
AGLY177
AARG334
AARG363

226707

PDB entries from 2024-10-30

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