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6PK4

cryoEM structure of the substrate-bound human CTP synthase 2 filament

Functional Information from GO Data
ChainGOidnamespacecontents
A0003883molecular_functionCTP synthase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006220biological_processpyrimidine nucleotide metabolic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006241biological_processCTP biosynthetic process
A0006541biological_processglutamine metabolic process
A0016874molecular_functionligase activity
A0019637biological_processorganophosphate metabolic process
A0019856biological_processpyrimidine nucleobase biosynthetic process
A0042802molecular_functionidentical protein binding
A0044210biological_process'de novo' CTP biosynthetic process
A0097268cellular_componentcytoophidium
B0003883molecular_functionCTP synthase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006220biological_processpyrimidine nucleotide metabolic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006241biological_processCTP biosynthetic process
B0006541biological_processglutamine metabolic process
B0016874molecular_functionligase activity
B0019637biological_processorganophosphate metabolic process
B0019856biological_processpyrimidine nucleobase biosynthetic process
B0042802molecular_functionidentical protein binding
B0044210biological_process'de novo' CTP biosynthetic process
B0097268cellular_componentcytoophidium
C0003883molecular_functionCTP synthase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006220biological_processpyrimidine nucleotide metabolic process
C0006221biological_processpyrimidine nucleotide biosynthetic process
C0006241biological_processCTP biosynthetic process
C0006541biological_processglutamine metabolic process
C0016874molecular_functionligase activity
C0019637biological_processorganophosphate metabolic process
C0019856biological_processpyrimidine nucleobase biosynthetic process
C0042802molecular_functionidentical protein binding
C0044210biological_process'de novo' CTP biosynthetic process
C0097268cellular_componentcytoophidium
D0003883molecular_functionCTP synthase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006220biological_processpyrimidine nucleotide metabolic process
D0006221biological_processpyrimidine nucleotide biosynthetic process
D0006241biological_processCTP biosynthetic process
D0006541biological_processglutamine metabolic process
D0016874molecular_functionligase activity
D0019637biological_processorganophosphate metabolic process
D0019856biological_processpyrimidine nucleobase biosynthetic process
D0042802molecular_functionidentical protein binding
D0044210biological_process'de novo' CTP biosynthetic process
D0097268cellular_componentcytoophidium
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue UTP A 601
ChainResidue
ASER12
BLYS195
BLYS229
CGLN112
ALYS38
ATYR42
AHIS55
AASP70
AGLY149
AATP602
BLYS193
BTHR194

site_idAC2
Number of Residues11
Detailsbinding site for residue ATP A 602
ChainResidue
ALYS16
AGLY17
AILE18
ALYS38
AASP70
AGLU146
AARG217
AVAL253
AASP312
AUTP601
BTHR189

site_idAC3
Number of Residues11
Detailsbinding site for residue ATP B 602
ChainResidue
ATHR189
BLYS16
BGLY17
BILE18
BLYS38
BASP70
BGLU146
BARG217
BVAL253
BASP312
BUTP601

site_idAC4
Number of Residues11
Detailsbinding site for residue ATP C 602
ChainResidue
CLYS16
CGLY17
CILE18
CLYS38
CASP70
CGLU146
CARG217
CVAL253
CASP312
CUTP601
DTHR189

site_idAC5
Number of Residues11
Detailsbinding site for residue ATP D 602
ChainResidue
CTHR189
DLYS16
DGLY17
DILE18
DLYS38
DASP70
DGLU146
DARG217
DVAL253
DASP312
DUTP601

site_idAC6
Number of Residues15
Detailsbinding site for Di-peptide UTP B 601 and HIS B 55
ChainResidue
ALYS193
ATHR194
ALYS195
ALYS229
BSER12
BLYS38
BTYR42
BTYR53
BGLU54
BGLY56
BASP68
BASP70
BGLY149
BATP602
DGLN112

site_idAC7
Number of Residues15
Detailsbinding site for Di-peptide UTP B 601 and HIS B 55
ChainResidue
ALYS193
ATHR194
ALYS195
ALYS229
BSER12
BLYS38
BTYR42
BTYR53
BGLU54
BGLY56
BASP68
BASP70
BGLY149
BATP602
DGLN112

site_idAC8
Number of Residues15
Detailsbinding site for Di-peptide UTP C 601 and HIS C 55
ChainResidue
DLYS195
DLYS229
AGLN112
CSER12
CLYS38
CTYR42
CTYR53
CGLU54
CGLY56
CASP68
CASP70
CGLY149
CATP602
DLYS193
DTHR194

site_idAC9
Number of Residues15
Detailsbinding site for Di-peptide UTP C 601 and HIS C 55
ChainResidue
AGLN112
CSER12
CLYS38
CTYR42
CTYR53
CGLU54
CGLY56
CASP68
CASP70
CGLY149
CATP602
DLYS193
DTHR194
DLYS195
DLYS229

site_idAD1
Number of Residues15
Detailsbinding site for Di-peptide UTP D 601 and HIS D 55
ChainResidue
BGLN112
CLYS193
CTHR194
CLYS195
CLYS229
DSER12
DLYS38
DTYR42
DTYR53
DGLU54
DGLY56
DASP68
DASP70
DGLY149
DATP602

site_idAD2
Number of Residues15
Detailsbinding site for Di-peptide UTP D 601 and HIS D 55
ChainResidue
BGLN112
CLYS193
CTHR194
CLYS195
CLYS229
DSER12
DLYS38
DTYR42
DTYR53
DGLU54
DGLY56
DASP68
DASP70
DGLY149
DATP602

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: For GATase activity => ECO:0000255|PROSITE-ProRule:PRU00605
ChainResidueDetails
ACYS399
DCYS399
DHIS526
DGLU528
AHIS526
AGLU528
BCYS399
BHIS526
BGLU528
CCYS399
CHIS526
CGLU528

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER568
BSER568
CSER568
DSER568

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER571
BSER571
CSER571
DSER571

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER574
BSER574
CSER574
DSER574

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PDB entries from 2024-07-24

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