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2BE9

Crystal structure of the CTP-liganded (T-State) aspartate transcarbamoylase from the extremely thermophilic archaeon Sulfolobus acidocaldarius

Functional Information from GO Data
ChainGOidnamespacecontents
A0004070molecular_functionaspartate carbamoyltransferase activity
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006520biological_processamino acid metabolic process
A0016597molecular_functionamino acid binding
A0016740molecular_functiontransferase activity
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
A0044205biological_process'de novo' UMP biosynthetic process
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0009347cellular_componentaspartate carbamoyltransferase complex
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1113
ChainResidue
BCYS113
BCYS118
BCYS142
BCYS145

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1114
ChainResidue
BLYS60
BHIS23
BSER54
BLYS55
BLYS55
BLYS56

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CTP B 401
ChainResidue
BLYS14
BILE15
BVAL20
BASP22
BHIS23
BLYS55
BLYS64
BASN88
BVAL90
BTYR93
BVAL95
BLYS98

Functional Information from PROSITE/UniProt
site_idPS00097
Number of Residues8
DetailsCARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEpSTRT
ChainResidueDetails
APHE45-THR52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1at1
ChainResidueDetails
AARG51
ATHR52
AARG101
AHIS129

238895

PDB entries from 2025-07-16

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