Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5MY2

KS-MAT DI-DOMAIN OF MOUSE FAS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
A0006633biological_processfatty acid biosynthetic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
B0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
B0006633biological_processfatty acid biosynthetic process
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
C0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
C0006633biological_processfatty acid biosynthetic process
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
D0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
D0006633biological_processfatty acid biosynthetic process
D0016740molecular_functiontransferase activity
D0016746molecular_functionacyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue COA D 900
ChainResidue
DMET499
DLEU766
DLEU767
DLYS772
DARG773
DHIS580
DMET620
DALA622
DASN644
DASP647
DTHR648
DTHR650
DPHE671

Functional Information from PROSITE/UniProt
site_idPS00606
Number of Residues17
DetailsKS3_1 Ketosynthase family 3 (KS3) active site signature. GPSiaLDtACSSSllAL
ChainResidueDetails
AGLY152-LEU168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues776
DetailsRegion: {"description":"Acyl and malonyl transferases"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsActive site: {"description":"For beta-ketoacyl synthase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"For malonyltransferase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU10022","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31811668","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6ROP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P49327","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues15
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P49327","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

PDB statisticsPDBj update infoContact PDBjnumon