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1RAH

CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY

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
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006520biological_processamino acid metabolic process
A0006541biological_processglutamine metabolic process
A0009347cellular_componentaspartate carbamoyltransferase complex
A0016597molecular_functionamino acid binding
A0016740molecular_functiontransferase activity
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
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
B0046872molecular_functionmetal ion binding
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
C0006221biological_processpyrimidine nucleotide biosynthetic process
C0006520biological_processamino acid metabolic process
C0006541biological_processglutamine metabolic process
C0009347cellular_componentaspartate carbamoyltransferase complex
C0016597molecular_functionamino acid binding
C0016740molecular_functiontransferase activity
C0016743molecular_functioncarboxyl- or carbamoyltransferase activity
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
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 154
ChainResidue
BCYS114
BCYS138
BCYS141
BCYS109

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 154
ChainResidue
DCYS109
DCYS114
DCYS138
DCYS141

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CTP B 999
ChainResidue
BVAL9
BALA11
BILE12
BHIS20
BLYS60
BILE86
BTYR89
BLYS94

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CTP D 999
ChainResidue
DGLU10
DALA11
DILE12
DASP19
DTHR82
DASN84
DTYR89
DGLU90
DVAL91
DLYS94

site_idZNB
Number of Residues4
DetailsZN BINDING SITE OF CHAIN B
ChainResidue
BCYS109
BCYS114
BCYS138
BCYS141

site_idZND
Number of Residues4
DetailsZN BINDING SITE OF CHAIN D
ChainResidue
DCYS109
DCYS114
DCYS138
DCYS141

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_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
BCYS109
CARG105
CHIS134
CGLN137
CLEU267
CPRO268
BCYS114
BCYS138
BCYS141
DCYS109
DCYS114
DCYS138
DCYS141
CTHR55

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
ChainResidueDetails
ALYS84
AARG167
AARG229
CLYS84
CARG167
CARG229

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1at1
ChainResidueDetails
AARG54
AHIS134
AARG105
ATHR55

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1at1
ChainResidueDetails
CARG54
CHIS134
CARG105
CTHR55

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 2024-10-30

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