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8W7D

Crystal structure of EcPPAT-FR901483 complex

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
C0000287molecular_functionmagnesium ion binding
C0004044molecular_functionamidophosphoribosyltransferase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006164biological_processpurine nucleotide biosynthetic process
C0006189biological_process'de novo' IMP biosynthetic process
C0006541biological_processglutamine metabolic process
C0009113biological_processpurine nucleobase biosynthetic process
C0016757molecular_functionglycosyltransferase activity
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0097216molecular_functionguanosine tetraphosphate binding
D0000287molecular_functionmagnesium ion binding
D0004044molecular_functionamidophosphoribosyltransferase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006164biological_processpurine nucleotide biosynthetic process
D0006189biological_process'de novo' IMP biosynthetic process
D0006541biological_processglutamine metabolic process
D0009113biological_processpurine nucleobase biosynthetic process
D0016757molecular_functionglycosyltransferase activity
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLLVDDSIVRGtT
ChainResidueDetails
AVAL363-THR375

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:7037784
ChainResidueDetails
ACYS2
BCYS2
CCYS2
DCYS2

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01931
ChainResidueDetails
ATHR305
DTHR305
DASP367
DASP368
AASP367
AASP368
BTHR305
BASP367
BASP368
CTHR305
CASP367
CASP368

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 214
ChainResidueDetails
ACYS2covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AGLY28activator, electrostatic stabiliser, hydrogen bond acceptor
AASN102electrostatic stabiliser, hydrogen bond donor
AGLY103electrostatic stabiliser, hydrogen bond donor
ATYR259electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 214
ChainResidueDetails
BCYS2covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
BGLY28activator, electrostatic stabiliser, hydrogen bond acceptor
BASN102electrostatic stabiliser, hydrogen bond donor
BGLY103electrostatic stabiliser, hydrogen bond donor
BTYR259electrostatic stabiliser, hydrogen bond donor

site_idMCSA3
Number of Residues5
DetailsM-CSA 214
ChainResidueDetails
CCYS2covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
CGLY28activator, electrostatic stabiliser, hydrogen bond acceptor
CASN102electrostatic stabiliser, hydrogen bond donor
CGLY103electrostatic stabiliser, hydrogen bond donor
CTYR259electrostatic stabiliser, hydrogen bond donor

site_idMCSA4
Number of Residues5
DetailsM-CSA 214
ChainResidueDetails
DCYS2covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
DGLY28activator, electrostatic stabiliser, hydrogen bond acceptor
DASN102electrostatic stabiliser, hydrogen bond donor
DGLY103electrostatic stabiliser, hydrogen bond donor
DTYR259electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-08-14

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