Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2BYY

E.coli KAS I H298E Mutation

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
C0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006633biological_processfatty acid biosynthetic process
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
C0044281biological_processsmall molecule metabolic process
C1903966biological_processmonounsaturated fatty acid biosynthetic process
D0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006633biological_processfatty acid biosynthetic process
D0016746molecular_functionacyltransferase activity
D0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
D0044281biological_processsmall molecule metabolic process
D1903966biological_processmonounsaturated fatty acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NH4 A 1406
ChainResidue
AASN296
ASER297
AGLU342
ASER387
AASN388

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NH4 B 1406
ChainResidue
BASN388
BASN296
BSER297
BGLU342
BSER387

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NH4 C 1406
ChainResidue
CASN296
CSER297
CGLU342
CSER387
CASN388

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NH4 D 1406
ChainResidue
DASN296
DSER297
DGLU342
DSER387
DASN388

Functional Information from PROSITE/UniProt
site_idPS00606
Number of Residues17
DetailsKS3_1 Ketosynthase family 3 (KS3) active site signature. GVNysISsACATSahCI
ChainResidueDetails
AGLY154-ILE170

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348, ECO:0000305|PubMed:10571059
ChainResidueDetails
ACYS163
BCYS163
CCYS163
DCYS163

site_idSWS_FT_FI2
Number of Residues8
DetailsACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348
ChainResidueDetails
AGLU298
AHIS333
BGLU298
BHIS333
CGLU298
CHIS333
DGLU298
DHIS333

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 292
ChainResidueDetails
ACYS163activator, covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile
AGLU298electrostatic 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

site_idMCSA2
Number of Residues6
DetailsM-CSA 292
ChainResidueDetails
BCYS163activator, covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile
BGLU298electrostatic 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_idMCSA3
Number of Residues6
DetailsM-CSA 292
ChainResidueDetails
CCYS163activator, covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile
CGLU298electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
CLYS328activator, hydrogen bond donor
CHIS333electrostatic stabiliser, hydrogen bond donor, increase basicity
CPHE390activator, hydrogen bond acceptor
CPHE392electrostatic stabiliser, hydrogen bond donor

site_idMCSA4
Number of Residues6
DetailsM-CSA 292
ChainResidueDetails
DCYS163activator, covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile
DGLU298electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
DLYS328activator, hydrogen bond donor
DHIS333electrostatic stabiliser, hydrogen bond donor, increase basicity
DPHE390activator, hydrogen bond acceptor
DPHE392electrostatic stabiliser, hydrogen bond donor

site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dd8
ChainResidueDetails
APHE392
ALYS328
AGLU298
AHIS333
APHE390
ACYS163

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dd8
ChainResidueDetails
BPHE392
BLYS328
BGLU298
BHIS333
BPHE390
BCYS163

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dd8
ChainResidueDetails
CPHE392
CLYS328
CGLU298
CHIS333
CPHE390
CCYS163

site_idCSA4
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dd8
ChainResidueDetails
DPHE392
DLYS328
DGLU298
DHIS333
DPHE390
DCYS163

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon