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5KOF

Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and Acyl Carrier Protein, AcpP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006633biological_processfatty acid biosynthetic process
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0044281biological_processsmall molecule metabolic process
A1903966biological_processmonounsaturated fatty acid biosynthetic process
B0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006633biological_processfatty acid biosynthetic process
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0044281biological_processsmall molecule metabolic process
B1903966biological_processmonounsaturated fatty acid biosynthetic process
C0000035molecular_functionacyl binding
C0000036molecular_functionacyl carrier activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006633biological_processfatty acid biosynthetic process
C0008289molecular_functionlipid binding
C0008610biological_processlipid biosynthetic process
C0009245biological_processlipid A biosynthetic process
C0009410biological_processresponse to xenobiotic stimulus
C0031177molecular_functionphosphopantetheine binding
D0000035molecular_functionacyl binding
D0000036molecular_functionacyl carrier activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006633biological_processfatty acid biosynthetic process
D0008289molecular_functionlipid binding
D0008610biological_processlipid biosynthetic process
D0009245biological_processlipid A biosynthetic process
D0009410biological_processresponse to xenobiotic stimulus
D0031177molecular_functionphosphopantetheine binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue 6W5 C 101
ChainResidue
BCYS163
BHIS333
BPHE390
BPHE392
CSER36
BMET204
BGLY205
BALA206
BVAL270
BHIS298
BTHR300
BTHR302
BVAL304

site_idAC2
Number of Residues15
Detailsbinding site for Di-peptide 6W5 D 101 and SER D 36
ChainResidue
ACYS163
AGLY205
AVAL270
AHIS298
ATHR300
ATHR302
AGLY305
AHIS333
APHE390
APHE392
DASP35
DLEU37
DASP38
DVAL40
DHOH201

site_idAC3
Number of Residues24
Detailsbinding site for Di-peptide 6W5 D 101 and CYS A 163
ChainResidue
AMET79
AGLY100
AILE102
ASER143
AVAL155
AASN156
ATYR157
ASER161
AALA162
AALA164
ATHR165
APHE186
AGLY205
AVAL270
AHIS298
ATHR300
ATHR302
AGLY305
AHIS333
ALEU335
APHE390
APHE392
DSER36
DHOH201

Functional Information from PROSITE/UniProt
site_idPS00012
Number of Residues16
DetailsPHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGADSLDTVELVMAL
ChainResidueDetails
CASP31-LEU46

site_idPS00606
Number of Residues17
DetailsKS3_1 Ketosynthase family 3 (KS3) active site signature. GVNysISsACATSahCI
ChainResidueDetails
BGLY154-ILE170

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|PROSITE-ProRule:PRU00258, ECO:0000269|PubMed:4882207
ChainResidueDetails
CSER36
DSER36

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348
ChainResidueDetails
BHIS298
BHIS333
AHIS298
AHIS333

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 292
ChainResidueDetails
BCYS163activator, covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile
BHIS298electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BLYS328activator, hydrogen bond donor
BHIS333electrostatic stabiliser, hydrogen bond donor, increase basicity
BPHE390activator, hydrogen bond acceptor
BPHE392electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues6
DetailsM-CSA 292
ChainResidueDetails
ACYS163activator, covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile
AHIS298electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS328activator, hydrogen bond donor
AHIS333electrostatic stabiliser, hydrogen bond donor, increase basicity
APHE390activator, hydrogen bond acceptor
APHE392electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-07-17

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