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1A3C

PYRR, THE BACILLUS SUBTILIS PYRIMIDINE BIOSYNTHETIC OPERON REPRESSOR, DIMERIC FORM

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0004845molecular_functionuracil phosphoribosyltransferase activity
A0006353biological_processDNA-templated transcription termination
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SM A 182
ChainResidue
AGLU10
AGLU10
AASP167
AASP167
AASP173
AASP173

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SM A 183
ChainResidue
AHOH325
AHOH335

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 184
ChainResidue
ALYS40
AASP105
AVAL107
ALEU108
ATYR109
ATHR110
AGLY111
AARG112
ATHR113
AVAL114
AHOH261

site_idPRA
Number of Residues10
DetailsDUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE.
ChainResidue
AASP105
ALYS40
AASP106
AVAL107
ALEU108
ATYR109
ATHR110
AGLY111
AARG112
ATHR113

site_idSM1
Number of Residues4
DetailsSM3+ ION BINDING SITE. THE SM3+ ION LIES ON A CRYSTALLOGRAPHIC TWO-FOLD AXIS, AND ISOCTAHEDRALLY COORDINATED BY THE OXYGENS OF THREE AMINO ACID SIDE CHAINS AND THEIR SYMMETRY RELATED ATOMS.
ChainResidue
ASM182
AGLU10
AASP167
AASP173

site_idSM2
Number of Residues1
DetailsSM3+ ION BINDING SITE. THE SM3+ ION LIES ON A GENERAL POSITION AND IS COORDINATED BY WATERS.
ChainResidue
ASM183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATHR41
AASP105
AARG138
AVAL162

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PDB entries from 2024-04-24

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