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

4KGZ

The R state structure of E. coli ATCase with UTP and Magnesium bound

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
C0004070molecular_functionaspartate carbamoyltransferase activity
C0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
C0006520biological_processamino acid metabolic process
C0016597molecular_functionamino acid binding
C0016743molecular_functioncarboxyl- or carbamoyltransferase activity
D0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
D0009347cellular_componentaspartate carbamoyltransferase complex
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PAL A 401
ChainResidue
ASER52
AARG229
AGLN231
ALEU267
AHOH506
AHOH538
ATHR53
AARG54
ATHR55
ASER80
ALYS84
AARG105
AHIS134
AARG167

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 201
ChainResidue
BCYS109
BCYS114
BCYS138
BCYS141

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE UTP B 202
ChainResidue
BALA11
BILE12
BVAL17
BHIS20
BLYS60
BTYR89
BLYS94
BUTP203
BMG204
BHOH301
BHOH302

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE UTP B 203
ChainResidue
BGLU10
BHIS20
BLEU48
BPRO49
BSER50
BGLU52
BLYS56
BLYS60
BUTP202
BMG204
BHOH301
BHOH302
DARG41

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 204
ChainResidue
BUTP202
BUTP203
BHOH301
BHOH302

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PAL C 401
ChainResidue
CSER52
CTHR53
CARG54
CTHR55
CSER80
CLYS84
CARG105
CHIS134
CARG167
CTHR168
CARG229
CGLN231
CLEU267
CHOH509
CHOH528
CHOH531

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 201
ChainResidue
DCYS109
DCYS114
DCYS138
DCYS141

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE UTP D 202
ChainResidue
DALA11
DILE12
DHIS20
DLYS60
DTYR89
DLYS94
DUTP203
DMG204
DHOH301
DHOH302
DHOH318

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE UTP D 203
ChainResidue
BARG41
DHIS20
DLEU48
DPRO49
DSER50
DGLY51
DGLU52
DLYS56
DLEU58
DLYS60
DUTP202
DMG204
DHOH301
DHOH302

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 204
ChainResidue
DUTP202
DUTP203
DHOH301
DHOH302

Functional Information from PROSITE/UniProt
site_idPS00097
Number of Residues8
DetailsCARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT
ChainResidueDetails
APHE48-THR55

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon