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2ATC

CRYSTAL AND MOLECULAR STRUCTURES OF NATIVE AND CTP-LIGANDED ASPARTATE CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0004070molecular_functionaspartate carbamoyltransferase activity
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006520biological_processamino acid metabolic process
A0016597molecular_functionamino acid binding
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0009347cellular_componentaspartate carbamoyltransferase complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 153
ChainResidue
BCYS109
BCYS114
BCYS137
BCYS140

site_idCTA
Number of Residues13
DetailsRESIDUES BELIEVED TO BE INVOLVED IN THE BINDING OF SUBSTRATES
ChainResidue
ASER52
ATYR165
AARG167
ALYS224
ATYR232
AARG54
ATHR55
ALYS83
ALYS84
AARG105
AGLY128
AHIS134
AGLN137

site_idRGB
Number of Residues2
DetailsRESIDUES WHICH BIND EFFECTOR MOLECULES
ChainResidue
BLYS6
BLEU7

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 Residues7
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3380787","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3380787","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

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

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

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PDB entries from 2025-07-23

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