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6OTT

Structure of PurF in complex with ppApp

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004044molecular_functionamidophosphoribosyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0006541biological_processglutamine metabolic process
A0009113biological_processpurine nucleobase biosynthetic process
A0016757molecular_functionglycosyltransferase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0097216molecular_functionguanosine tetraphosphate binding
B0000287molecular_functionmagnesium ion binding
B0004044molecular_functionamidophosphoribosyltransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0006541biological_processglutamine metabolic process
B0009113biological_processpurine nucleobase biosynthetic process
B0016757molecular_functionglycosyltransferase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue MG A 601
ChainResidue
AN7Y602
AN7Y602

site_idAC2
Number of Residues15
Detailsbinding site for residue N7Y A 602
ChainResidue
AHIS59
AARG62
AARG62
AALA82
ASER83
AGLU84
AMG601
AMG601
AARG45
AARG45
ALYS46
AALA47
AASN48
AARG58
AHIS59

site_idAC3
Number of Residues2
Detailsbinding site for residue MG B 601
ChainResidue
BN7Y602
BN7Y602

site_idAC4
Number of Residues15
Detailsbinding site for residue N7Y B 602
ChainResidue
BARG45
BARG45
BLYS46
BALA47
BASN48
BARG58
BHIS59
BHIS59
BARG62
BARG62
BALA82
BSER83
BGLU84
BMG601
BMG601

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLLVDDSIVRGtT
ChainResidueDetails
AVAL362-THR374

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:7037784
ChainResidueDetails
ACYS1
BCYS1

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01931
ChainResidueDetails
ATHR304
AASP366
AASP367
BTHR304
BASP366
BASP367

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 214
ChainResidueDetails
ACYS1covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AGLY27activator, electrostatic stabiliser, hydrogen bond acceptor
AASN101electrostatic stabiliser, hydrogen bond donor
AGLY102electrostatic stabiliser, hydrogen bond donor
ATYR258electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 214
ChainResidueDetails
BCYS1covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
BGLY27activator, electrostatic stabiliser, hydrogen bond acceptor
BASN101electrostatic stabiliser, hydrogen bond donor
BGLY102electrostatic stabiliser, hydrogen bond donor
BTYR258electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-07-17

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