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4QNR

CRYSTAL STRUCTURE OF PSPF(1-265) E108Q MUTANT bound to ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006355biological_processregulation of DNA-templated transcription
A0008134molecular_functiontranscription factor binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ATP A 301
ChainResidue
AASN7
ALYS42
AGLU43
ALEU44
AASP164
AILE226
AARG227
AMG302
AHOH426
AHOH470
AHOH511
ALEU8
AHOH537
AHOH546
AHOH592
ALEU9
APHE15
AGLU37
AARG38
AGLY39
ATHR40
AGLY41

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 302
ChainResidue
AGLU43
AASP107
AATP301
AHOH546

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
AHIS24
AARG239
AHOH407

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
APHE78
AGLY79
AHIS80
AGLU81
AGLU97
AGLU130
ALEU138
AHOH539
AHOH540

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EPE A 305
ChainResidue
AGLU81
AGLN108
AALA110
ATHR111
ASER135
ATHR148
AASN149

Functional Information from PROSITE/UniProt
site_idPS00688
Number of Residues10
DetailsSIGMA54_INTERACT_3 Sigma-54 interaction domain C-terminal part signature. WPGNIRELkN
ChainResidueDetails
ATRP222-ASN231

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00193","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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