Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6JDL

Central domain of FleQ H287A mutant 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 Residues23
Detailsbinding site for residue AGS A 401
ChainResidue
ASER145
AVAL182
AASP245
AARG334
AVAL362
AARG363
AMG402
AHOH504
AHOH505
AHOH506
AHOH509
ALEU146
AHOH516
AHOH534
AHOH541
AHOH555
AVAL147
ASER176
AGLY177
ATHR178
AGLY179
ALYS180
AGLU181

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 402
ChainResidue
AGLU181
AAGS401
AHOH516
AHOH534

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
AASN186
AGLU330
ALEU142

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

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon