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

6FBA

Crystal Structure of truncated aspartate transcarbamoylase from Plasmodium falciparum with bound inhibitor 2,3-naphthalenediol

Functional Information from GO Data
ChainGOidnamespacecontents
A0004070molecular_functionaspartate carbamoyltransferase activity
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006520biological_processamino acid metabolic process
A0016020cellular_componentmembrane
A0016597molecular_functionamino acid binding
A0016740molecular_functiontransferase activity
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
A0044205biological_process'de novo' UMP biosynthetic process
B0004070molecular_functionaspartate carbamoyltransferase activity
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006520biological_processamino acid metabolic process
B0016020cellular_componentmembrane
B0016597molecular_functionamino acid binding
B0016740molecular_functiontransferase activity
B0016743molecular_functioncarboxyl- or carbamoyltransferase activity
B0044205biological_process'de novo' UMP biosynthetic process
C0004070molecular_functionaspartate carbamoyltransferase activity
C0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
C0006221biological_processpyrimidine nucleotide biosynthetic process
C0006520biological_processamino acid metabolic process
C0016020cellular_componentmembrane
C0016597molecular_functionamino acid binding
C0016740molecular_functiontransferase activity
C0016743molecular_functioncarboxyl- or carbamoyltransferase activity
C0044205biological_process'de novo' UMP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 401
ChainResidue
AGLY122
ALYS124
BLYS124
BSO4401
CGLY122
CLYS124

site_idAC2
Number of Residues7
Detailsbinding site for residue D48 A 402
ChainResidue
ALEU149
ATYR152
BARG109
BPRO335
AGLU140
AALA145
AILE148

site_idAC3
Number of Residues4
Detailsbinding site for residue DMS A 403
ChainResidue
ATHR77
AILE84
ATYR93
ATYR368

site_idAC4
Number of Residues10
Detailsbinding site for residue MLI A 404
ChainResidue
AARG109
ATHR110
ASER113
AGLN190
APRO333
AARG363
AHOH505
AHOH509
CTYR152
CD48401

site_idAC5
Number of Residues6
Detailsbinding site for residue MLI A 405
ChainResidue
ASER107
ATHR108
AARG109
ATHR110
AARG295
CLYS138

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 406
ChainResidue
APHE103
AGLU105
ASER107
ATHR108
AARG111
ATHR129

site_idAC7
Number of Residues6
Detailsbinding site for residue NA A 407
ChainResidue
AHOH517
AHOH529
BHOH535
BHOH541
CHOH509
CHOH556

site_idAC8
Number of Residues10
Detailsbinding site for residue SO4 B 401
ChainResidue
ALEU119
ALYS124
ASO4401
BLEU119
BLYS124
BHOH504
BHOH505
BHOH514
CLEU119
CLYS124

site_idAC9
Number of Residues9
Detailsbinding site for residue D48 B 402
ChainResidue
BGLU140
BALA145
BILE148
BLEU149
BTYR152
BHOH527
CARG109
CLEU334
CPRO335

site_idAD1
Number of Residues3
Detailsbinding site for residue DMS B 403
ChainResidue
BILE84
BTYR368
BHOH538

site_idAD2
Number of Residues6
Detailsbinding site for residue PEG B 404
ChainResidue
BGLY139
BTHR141
BASP144
CARG336
CVAL337
CVAL342

site_idAD3
Number of Residues5
Detailsbinding site for residue D48 C 401
ChainResidue
AARG109
ALEU334
AMLI404
CGLU140
CILE148

site_idAD4
Number of Residues1
Detailsbinding site for residue DMS C 402
ChainResidue
CTYR368

site_idAD5
Number of Residues5
Detailsbinding site for residue PEG C 403
ChainResidue
AVAL342
AASP345
CTHR141
CGLU143
CASP144

site_idAD6
Number of Residues6
Detailsbinding site for residue MLI C 404
ChainResidue
BLYS138
CPRO106
CSER107
CTHR108
CARG109
CTHR110

site_idAD7
Number of Residues3
Detailsbinding site for residue GOL C 405
ChainResidue
CARG325
CASP326
CASP327

Functional Information from PROSITE/UniProt
site_idPS00097
Number of Residues8
DetailsCARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FlEpSTRT
ChainResidueDetails
APHE103-THR110
CPHE103-THR110

site_idPS00181
Number of Residues17
DetailsGLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPIinag.NGTGeHptqS
ChainResidueDetails
ALYS175-SER191
CLYS175-SER191

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon