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6PCC

Crystal structure of beta-ketoadipyl-CoA thiolase mutant (H356A) in complex hexanoyl coenzyme A

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 Residues19
Detailsbinding site for residue COA A 1001
ChainResidue
ACYS90
AASN322
APHE325
ALEU358
AHOH1103
AHOH1206
AHOH1252
AHOH1256
AHOH1309
AHOH1319
BHOH790
AILE145
AMET163
AARG226
ATHR229
AALA249
AGLY250
ASER253
AGLY254

site_idAC2
Number of Residues12
Detailsbinding site for residue O8Y A 1002
ChainResidue
AASN58
ATHR143
ATHR144
AILE145
AGLY146
AARG148
AMET163
ALEU358
AHOH1114
AHOH1147
AHOH1169
DARG65

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 1003
ChainResidue
AARG187
ASER188
ALYS191
AGLU323
AVAL345
AASN346
AGLY349
AHOH1102

site_idAC4
Number of Residues11
Detailsbinding site for residue O8Y B 502
ChainResidue
BASN58
BLEU89
BTHR143
BILE145
BGLY146
BARG148
BMET163
BLEU358
BHOH694
BHOH780
CARG65

site_idAC5
Number of Residues9
Detailsbinding site for residue GOL B 503
ChainResidue
BARG187
BSER188
BLYS191
BGLU323
BASP340
BVAL345
BASN346
BGLY349
BHOH624

site_idAC6
Number of Residues12
Detailsbinding site for residue O8Y C 502
ChainResidue
BARG65
CALA57
CASN58
CLEU89
CTHR143
CTHR144
CILE145
CGLY146
CARG148
CLEU358
CHOH682
CHOH806

site_idAC7
Number of Residues11
Detailsbinding site for residue GOL C 503
ChainResidue
CPHE184
CARG187
CSER188
CLYS191
CGLU323
CASP340
CASP341
CVAL345
CASN346
CGLY349
CHOH644

site_idAC8
Number of Residues9
Detailsbinding site for residue O8Y D 502
ChainResidue
AARG65
DASN58
DLEU89
DTHR143
DILE145
DGLY146
DARG148
DLEU358
DHOH825

site_idAC9
Number of Residues9
Detailsbinding site for residue GOL D 503
ChainResidue
DHOH641
DPHE184
DARG187
DSER188
DLYS191
DGLU323
DVAL345
DASN346
DGLY349

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

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PDB entries from 2024-08-21

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