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2BE7

Crystal structure of the unliganded (T-state) aspartate transcarbamoylase of the psychrophilic bacterium Moritella profunda

Functional Information from GO Data
ChainGOidnamespacecontents
A0004070molecular_functionaspartate carbamoyltransferase activity
A0005829cellular_componentcytosol
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006520biological_processamino acid metabolic process
A0009220biological_processpyrimidine ribonucleotide biosynthetic process
A0016597molecular_functionamino acid binding
A0016740molecular_functiontransferase activity
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
A0044205biological_process'de novo' UMP biosynthetic process
B0004070molecular_functionaspartate carbamoyltransferase activity
B0005829cellular_componentcytosol
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006520biological_processamino acid metabolic process
B0009220biological_processpyrimidine ribonucleotide biosynthetic process
B0016597molecular_functionamino acid binding
B0016740molecular_functiontransferase activity
B0016743molecular_functioncarboxyl- or carbamoyltransferase activity
B0044205biological_process'de novo' UMP biosynthetic process
C0004070molecular_functionaspartate carbamoyltransferase activity
C0005829cellular_componentcytosol
C0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
C0006221biological_processpyrimidine nucleotide biosynthetic process
C0006520biological_processamino acid metabolic process
C0009220biological_processpyrimidine ribonucleotide biosynthetic process
C0016597molecular_functionamino acid binding
C0016740molecular_functiontransferase activity
C0016743molecular_functioncarboxyl- or carbamoyltransferase activity
C0044205biological_process'de novo' UMP biosynthetic process
D0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
D0006221biological_processpyrimidine nucleotide biosynthetic process
D0009347cellular_componentaspartate carbamoyltransferase complex
D0046872molecular_functionmetal ion binding
E0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
E0006221biological_processpyrimidine nucleotide biosynthetic process
E0009347cellular_componentaspartate carbamoyltransferase complex
E0046872molecular_functionmetal ion binding
F0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
F0006221biological_processpyrimidine nucleotide biosynthetic process
F0009347cellular_componentaspartate carbamoyltransferase complex
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1108
ChainResidue
DCYS108
DCYS113
DCYS137
DCYS140

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 1108
ChainResidue
ECYS108
ECYS113
ECYS137
ECYS140

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 1108
ChainResidue
FCYS113
FCYS137
FCYS140
FCYS108

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 311
ChainResidue
ASER53
ATHR54
AARG55
ATHR56
BSER81

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 311
ChainResidue
ASER81
CSER53
CTHR54
CARG55
CTHR56
CHOH313

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 311
ChainResidue
BSER53
BTHR54
BARG55
BTHR56
BHOH320
CSER81

Functional Information from PROSITE/UniProt
site_idPS00097
Number of Residues8
DetailsCARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT
ChainResidueDetails
APHE49-THR56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI3
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1at1
ChainResidueDetails
AARG106
ATHR56
AHIS134
AARG55

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1at1
ChainResidueDetails
BARG106
BTHR56
BHIS134
BARG55

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1at1
ChainResidueDetails
CARG106
CTHR56
CHIS134
CARG55

239803

PDB entries from 2025-08-06

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