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3R7D

Crystal Structure of Unliganded Aspartate Transcarbamoylase from Bacillus subtilis

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
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
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
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 Residues12
DetailsBINDING SITE FOR RESIDUE PO4 A 305
ChainResidue
AASN67
BASN67
BHOH313
CASN67
AHOH319
AHOH323
AHOH328
AHOH334
AHOH367
AHOH385
AHOH388
AHOH411

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 306
ChainResidue
ASER11
ATHR12
AARG171
AHOH312
AHOH343

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 307
ChainResidue
ATHR73
ASER74
ALYS77
CSER47
CTHR48
CARG49
CPRO251

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 305
ChainResidue
BSER11
BTHR12
BARG171
BHOH372
BHOH484

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 C 305
ChainResidue
CLYS272
CLYS275
CHOH357
CHOH381

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 C 306
ChainResidue
CSER11
CTHR12
CARG171
CHOH359
CHOH573

Functional Information from PROSITE/UniProt
site_idPS00097
Number of Residues8
DetailsCARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEpSTRT
ChainResidueDetails
APHE43-THR50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00001
ChainResidueDetails
AARG49
APRO251
BARG49
BTHR50
BLYS77
BARG99
BHIS127
BGLN130
BARG160
BARG211
BALA250
ATHR50
BPRO251
CARG49
CTHR50
CLYS77
CARG99
CHIS127
CGLN130
CARG160
CARG211
CALA250
ALYS77
CPRO251
AARG99
AHIS127
AGLN130
AARG160
AARG211
AALA250

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17218307
ChainResidueDetails
ASER303
BSER303
CSER303

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PDB entries from 2024-07-10

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