2AIR

T-state Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-alanosine Ligated Enzyme

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Functional Information from GO Data

ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0016597molecular_functionamino acid binding
A0004070molecular_functionaspartate carbamoyltransferase activity
A0042802molecular_functionidentical protein binding
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0044205biological_process'de novo' UMP biosynthetic process
A0006520biological_processcellular amino acid metabolic process
A0006807biological_processnitrogen compound metabolic process
A0070207biological_processprotein homotrimerization
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0016597molecular_functionamino acid binding
G0004070molecular_functionaspartate carbamoyltransferase activity
G0042802molecular_functionidentical protein binding
G0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
G0044205biological_process'de novo' UMP biosynthetic process
G0006520biological_processcellular amino acid metabolic process
G0006807biological_processnitrogen compound metabolic process
G0070207biological_processprotein homotrimerization
B0009347cellular_componentaspartate carbamoyltransferase complex
B0005737cellular_componentcytoplasm
B0008270molecular_functionzinc ion binding
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
H0009347cellular_componentaspartate carbamoyltransferase complex
H0005737cellular_componentcytoplasm
H0008270molecular_functionzinc ion binding
H0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
H0006221biological_processpyrimidine nucleotide biosynthetic process
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
AC14BINDING SITE FOR RESIDUE ZN B 800
ChainResidue
BCYS109
BCYS114
BCYS138
BCYS141

AC24BINDING SITE FOR RESIDUE ZN H 801
ChainResidue
HCYS109
HCYS114
HCYS138
HCYS141

AC35BINDING SITE FOR RESIDUE CP A 802
ChainResidue
AARG54
ATHR55
AARG105
AHIS134
AAL0805

AC46BINDING SITE FOR RESIDUE CP G 803
ChainResidue
GARG54
GTHR55
GARG105
GHIS134
GARG229
GAL0804

AC57BINDING SITE FOR RESIDUE AL0 G 804
ChainResidue
GALA51
GSER52
GARG54
GTHR55
GSER80
GARG105
GCP803

AC67BINDING SITE FOR RESIDUE AL0 A 805
ChainResidue
AALA51
ASER52
ATHR53
AARG54
ASER80
AARG105
ACP802

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
PS0009716Aspartate and ornithine carbamoyltransferases signature.F-x-[EK]-x-S-[GT]-R-T.
ChainResidueDetails
APHE48-THR55
GPHE48-THR55

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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
CSA14Annotated By Reference To The Literature 1at1
ChainResidueDetails
AARG54
AHIS134
AARG105
ATHR55

CSA24Annotated By Reference To The Literature 1at1
ChainResidueDetails
GARG54
GHIS134
GARG105
GTHR55

?

Catalytic Information from CSA

site_idNumber of ResiduesDetails
CSA14Annotated By Reference To The Literature 1at1
ChainResidueDetails
AARG54
AHIS134
AARG105
ATHR55

CSA24Annotated By Reference To The Literature 1at1
ChainResidueDetails
GARG54
GHIS134
GARG105
GTHR55

167518
PDB entries from 2020-08-12