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6TZV

Crystal Structure of the carboxyltransferase subunit of ACC (AccD6) in complex with inhibitor Phenyl-Cyclodiaone from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003989molecular_functionacetyl-CoA carboxylase activity
A0004658molecular_functionpropionyl-CoA carboxylase activity
A0005515molecular_functionprotein binding
A0006633biological_processfatty acid biosynthetic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0009317cellular_componentacetyl-CoA carboxylase complex
A0016740molecular_functiontransferase activity
A0016874molecular_functionligase activity
A0019367biological_processfatty acid elongation, saturated fatty acid
B0003989molecular_functionacetyl-CoA carboxylase activity
B0004658molecular_functionpropionyl-CoA carboxylase activity
B0005515molecular_functionprotein binding
B0006633biological_processfatty acid biosynthetic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0009317cellular_componentacetyl-CoA carboxylase complex
B0016740molecular_functiontransferase activity
B0016874molecular_functionligase activity
B0019367biological_processfatty acid elongation, saturated fatty acid
C0003989molecular_functionacetyl-CoA carboxylase activity
C0004658molecular_functionpropionyl-CoA carboxylase activity
C0005515molecular_functionprotein binding
C0006633biological_processfatty acid biosynthetic process
C0009274cellular_componentpeptidoglycan-based cell wall
C0009317cellular_componentacetyl-CoA carboxylase complex
C0016740molecular_functiontransferase activity
C0016874molecular_functionligase activity
C0019367biological_processfatty acid elongation, saturated fatty acid
D0003989molecular_functionacetyl-CoA carboxylase activity
D0004658molecular_functionpropionyl-CoA carboxylase activity
D0005515molecular_functionprotein binding
D0006633biological_processfatty acid biosynthetic process
D0009274cellular_componentpeptidoglycan-based cell wall
D0009317cellular_componentacetyl-CoA carboxylase complex
D0016740molecular_functiontransferase activity
D0016874molecular_functionligase activity
D0019367biological_processfatty acid elongation, saturated fatty acid
E0003989molecular_functionacetyl-CoA carboxylase activity
E0004658molecular_functionpropionyl-CoA carboxylase activity
E0005515molecular_functionprotein binding
E0006633biological_processfatty acid biosynthetic process
E0009274cellular_componentpeptidoglycan-based cell wall
E0009317cellular_componentacetyl-CoA carboxylase complex
E0016740molecular_functiontransferase activity
E0016874molecular_functionligase activity
E0019367biological_processfatty acid elongation, saturated fatty acid
F0003989molecular_functionacetyl-CoA carboxylase activity
F0004658molecular_functionpropionyl-CoA carboxylase activity
F0005515molecular_functionprotein binding
F0006633biological_processfatty acid biosynthetic process
F0009274cellular_componentpeptidoglycan-based cell wall
F0009317cellular_componentacetyl-CoA carboxylase complex
F0016740molecular_functiontransferase activity
F0016874molecular_functionligase activity
F0019367biological_processfatty acid elongation, saturated fatty acid
G0003989molecular_functionacetyl-CoA carboxylase activity
G0004658molecular_functionpropionyl-CoA carboxylase activity
G0005515molecular_functionprotein binding
G0006633biological_processfatty acid biosynthetic process
G0009274cellular_componentpeptidoglycan-based cell wall
G0009317cellular_componentacetyl-CoA carboxylase complex
G0016740molecular_functiontransferase activity
G0016874molecular_functionligase activity
G0019367biological_processfatty acid elongation, saturated fatty acid
H0003989molecular_functionacetyl-CoA carboxylase activity
H0004658molecular_functionpropionyl-CoA carboxylase activity
H0005515molecular_functionprotein binding
H0006633biological_processfatty acid biosynthetic process
H0009274cellular_componentpeptidoglycan-based cell wall
H0009317cellular_componentacetyl-CoA carboxylase complex
H0016740molecular_functiontransferase activity
H0016874molecular_functionligase activity
H0019367biological_processfatty acid elongation, saturated fatty acid
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue PKP A 501
ChainResidue
AGLY98
BLEU345
BGLY366
BALA370
BVAL391
AALA99
APHE115
AGLY137
AGLY138
ATYR141
BALA300
BTYR326
BGLY341

site_idAC2
Number of Residues15
Detailsbinding site for residue PKP B 501
ChainResidue
ALEU295
AALA300
ATYR326
AGLY341
ALEU345
AGLY365
AGLY366
AALA370
AMET392
BGLY98
BALA99
BPHE115
BGLY137
BGLY138
BTYR141

site_idAC3
Number of Residues13
Detailsbinding site for residue PKP C 501
ChainResidue
CGLY98
CALA99
CPHE115
CGLY137
CGLY138
CTYR141
DALA300
DTYR326
DGLY341
DLEU345
DGLY366
DALA370
DVAL391

site_idAC4
Number of Residues14
Detailsbinding site for residue PKP D 501
ChainResidue
CALA300
CTYR326
CGLY341
CLEU345
CGLY365
CGLY366
CALA370
CVAL391
DGLY98
DALA99
DPHE115
DGLY137
DGLY138
DTYR141

site_idAC5
Number of Residues14
Detailsbinding site for residue PKP E 501
ChainResidue
EGLY98
EALA99
EPHE115
EGLY137
EGLY138
ETYR141
FLEU295
FALA300
FTYR326
FGLY341
FLEU345
FGLY366
FALA370
FVAL391

site_idAC6
Number of Residues15
Detailsbinding site for residue PKP F 501
ChainResidue
ELEU295
EALA300
ETYR326
EGLY341
ELEU345
EGLY365
EGLY366
EALA370
EMET392
FGLY98
FALA99
FPHE115
FGLY137
FGLY138
FTYR141

site_idAC7
Number of Residues13
Detailsbinding site for residue PKP G 501
ChainResidue
GGLY98
GALA99
GPHE115
GGLY137
GGLY138
GTYR141
HALA300
HTYR326
HGLY341
HLEU345
HGLY366
HALA370
HVAL391

site_idAC8
Number of Residues12
Detailsbinding site for residue PKP H 501
ChainResidue
GGLY341
GLEU345
GGLY366
GALA370
HGLY98
HALA99
HPHE115
HGLY137
HGLY138
HTYR141
GALA300
GTYR326

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBINDING: BINDING => ECO:0007744|PDB:4G2R
ChainResidueDetails
GALA99
GGLY138
GHIS185
GTRP334
HALA99
HGLY138
HHIS185
HTRP334
ATRP334
BALA99
BGLY138
BHIS185
BTRP334
CALA99
CGLY138
CHIS185
CTRP334
DALA99
DGLY138
DHIS185
DTRP334
EALA99
EGLY138
EHIS185
ETRP334
FALA99
FGLY138
FHIS185
FTRP334
AALA99
AGLY138
AHIS185

site_idSWS_FT_FI2
Number of Residues8
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609
ChainResidueDetails
BTHR2
CTHR2
DTHR2
ETHR2
FTHR2
GTHR2
HTHR2
ATHR2

221051

PDB entries from 2024-06-12

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