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6PCA

Crystal structure of beta-ketoadipyl-CoA thiolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003988molecular_functionacetyl-CoA C-acyltransferase activity
A0006635biological_processfatty acid beta-oxidation
A0010124biological_processphenylacetate catabolic process
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0019619biological_process3,4-dihydroxybenzoate catabolic process
A0033812molecular_function3-oxoadipyl-CoA thiolase activity
B0003988molecular_functionacetyl-CoA C-acyltransferase activity
B0006635biological_processfatty acid beta-oxidation
B0010124biological_processphenylacetate catabolic process
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0019619biological_process3,4-dihydroxybenzoate catabolic process
B0033812molecular_function3-oxoadipyl-CoA thiolase activity
C0003988molecular_functionacetyl-CoA C-acyltransferase activity
C0006635biological_processfatty acid beta-oxidation
C0010124biological_processphenylacetate catabolic process
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
C0019619biological_process3,4-dihydroxybenzoate catabolic process
C0033812molecular_function3-oxoadipyl-CoA thiolase activity
D0003988molecular_functionacetyl-CoA C-acyltransferase activity
D0006635biological_processfatty acid beta-oxidation
D0010124biological_processphenylacetate catabolic process
D0016746molecular_functionacyltransferase activity
D0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
D0019619biological_process3,4-dihydroxybenzoate catabolic process
D0033812molecular_function3-oxoadipyl-CoA thiolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue GOL A 501
ChainResidue
AARG187
ASER188
ALYS191
AGLU323
AVAL345
AASN346
AGLY349
AHOH624

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 502
ChainResidue
ATHR143
ATHR144
AARG148
ALEU358
ACL505
AHOH643
DARG65
AASN58

site_idAC3
Number of Residues4
Detailsbinding site for residue ACT A 503
ChainResidue
AGLY128
ALYS129
DGLU62
DARG122

site_idAC4
Number of Residues3
Detailsbinding site for residue CL A 504
ChainResidue
AARG65
DGLY146
DGOL502

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 505
ChainResidue
AGLY146
AGOL502
DARG65

site_idAC6
Number of Residues8
Detailsbinding site for residue GOL B 501
ChainResidue
BARG187
BSER188
BLYS191
BGLU323
BVAL345
BASN346
BGLY349
BHOH620

site_idAC7
Number of Residues8
Detailsbinding site for residue GOL B 502
ChainResidue
BASN58
BTHR143
BTHR144
BGLY146
BARG148
BCL503
BHOH705
CARG65

site_idAC8
Number of Residues3
Detailsbinding site for residue CL B 503
ChainResidue
BGLY146
BGOL502
CARG65

site_idAC9
Number of Residues3
Detailsbinding site for residue CL B 504
ChainResidue
BARG65
CGLY146
CGOL502

site_idAD1
Number of Residues5
Detailsbinding site for residue CL B 505
ChainResidue
BPHE200
BGLU320
BASN348
BTHR368
BGLN372

site_idAD2
Number of Residues9
Detailsbinding site for residue GOL C 501
ChainResidue
CPHE184
CARG187
CSER188
CLYS191
CGLU323
CVAL345
CASN346
CGLY349
CHOH614

site_idAD3
Number of Residues7
Detailsbinding site for residue GOL C 502
ChainResidue
BARG65
BCL504
CASN58
CTHR143
CTHR144
CARG148
CHOH619

site_idAD4
Number of Residues5
Detailsbinding site for residue ACT C 503
ChainResidue
BGLU62
BARG122
CGLY128
CLYS129
CHOH731

site_idAD5
Number of Residues9
Detailsbinding site for residue GOL D 501
ChainResidue
DPHE184
DARG187
DSER188
DLYS191
DGLU323
DVAL345
DASN346
DGLY349
DHOH640

site_idAD6
Number of Residues7
Detailsbinding site for residue GOL D 502
ChainResidue
AARG65
ACL504
DASN58
DTHR143
DTHR144
DARG148
DHOH610

site_idAD7
Number of Residues5
Detailsbinding site for residue ACT D 503
ChainResidue
AGLU62
AARG122
DGLY128
DLYS129
DGLU131

Functional Information from PROSITE/UniProt
site_idPS00098
Number of Residues19
DetailsTHIOLASE_1 Thiolases acyl-enzyme intermediate signature. LNRlCASGMdAVgtafraI
ChainResidueDetails
ALEU86-ILE104

site_idPS00099
Number of Residues14
DetailsTHIOLASE_3 Thiolases active site. GLATMCVGvGqGlA
ChainResidueDetails
AGLY381-ALA394

site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NpnGGaIAlGHPlGmSG
ChainResidueDetails
AASN346-GLY362

224931

PDB entries from 2024-09-11

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