Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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 Residues4
DetailsBINDING:
ChainResidueDetails
BCYS109
BCYS114
BLYS138
BGLU141
ATHR138
ALEU262
APRO263

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
ChainResidueDetails
AGLY85
ATHR168
ASER230

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 405
ChainResidueDetails
ATHR55electrostatic stabiliser
AARG56electrostatic stabiliser, increase electrophilicity
AGLY85proton shuttle (general acid/base)
AHIS106electrostatic stabiliser, increase electrophilicity
APRO135electrostatic stabiliser, increase electrophilicity

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon