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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
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
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
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_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
DCYS108
FCYS113
FCYS137
FCYS140
BGLY86
BHIS107
BPRO135
BTHR138
BTHR168
BVAL230
BPRO268
DCYS113
BARG269
CTHR56
CARG57
CGLY86
CHIS107
CPRO135
CTHR138
CTHR168
CVAL230
CPRO268
DCYS137
CARG269
DCYS140
ECYS108
ECYS113
ECYS137
ECYS140
FCYS108

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

223532

PDB entries from 2024-08-07

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