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9EEH

Crystal structure of E. coli aspartate transcarbamoylase in the R-state complexed with PALA, ATP, GTP, and Mg2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004070molecular_functionaspartate carbamoyltransferase activity
A0004088molecular_functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006541biological_processL-glutamine metabolic process
A0009347cellular_componentaspartate carbamoyltransferase complex
A0042802molecular_functionidentical protein binding
A0044205biological_process'de novo' UMP biosynthetic process
A0070207biological_processprotein homotrimerization
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0008270molecular_functionzinc ion binding
B0009347cellular_componentaspartate carbamoyltransferase complex
C0004070molecular_functionaspartate carbamoyltransferase activity
C0004088molecular_functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
C0006541biological_processL-glutamine metabolic process
C0009347cellular_componentaspartate carbamoyltransferase complex
C0042802molecular_functionidentical protein binding
C0044205biological_process'de novo' UMP biosynthetic process
C0070207biological_processprotein homotrimerization
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
D0006221biological_processpyrimidine nucleotide biosynthetic process
D0008270molecular_functionzinc ion binding
D0009347cellular_componentaspartate carbamoyltransferase complex
Functional Information from PROSITE/UniProt
site_idPS00097
Number of Residues8
DetailsCARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT
ChainResidueDetails
APHE48-THR55

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3380787","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3380787","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 405
ChainResidueDetails
AARG54electrostatic stabiliser
ATHR55electrostatic stabiliser, increase electrophilicity
ALYS84proton shuttle (general acid/base)
AARG105electrostatic stabiliser, increase electrophilicity
AHIS134electrostatic stabiliser, increase electrophilicity

site_idMCSA2
Number of Residues5
DetailsM-CSA 405
ChainResidueDetails
CARG54electrostatic stabiliser
CTHR55electrostatic stabiliser, increase electrophilicity
CLYS84proton shuttle (general acid/base)
CARG105electrostatic stabiliser, increase electrophilicity
CHIS134electrostatic stabiliser, increase electrophilicity

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PDB entries from 2026-07-08

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