PDB 5c37 biological assemblies and structure analysis ‹ Protein Data Bank in Europe (PDBe)

Assemblies

Assembly 1

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Assembly Name: Fatty acid synthase
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Multimeric state: monomeric

Accessible surface area: 24815.2 Å²

Buried surface area: 1420.65 Å²

Dissociation area: 632.69 Å²

Dissociation energy (ΔG^diss): 0.32 kcal/mol

Dissociation entropy (TΔS^diss): 6.52 kcal/mol

Symmetry number: 1

PDBe Complex ID: PDB-CPX-155922

$Monomeric assembly 1 of PDB entry 5c37 coloured by chemically distinct molecules, front view. This structure contains: <ul class='image_legend_ul'><li class='image_legend_li'>1 copy of Fatty acid synthase;</li> <li class='image_legend_li'>1 copy of NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;</li> <li class='image_legend_li'>1 copy of 6-{[(3R)-1-(cyclopropylcarbonyl)pyrrolidin-3-yl]methyl}-5-[4-(1-methyl-1H-indazol-5-yl)phenyl]-4,6-diazaspiro[2.4]hept-4-en-7-one;</li> <li class='image_legend_li'>1 copy of CHLORIDE ION;</li> <li class='image_legend_li'>1 copy of water.</li></ul>}$

$Monomeric assembly 1 of PDB entry 5c37 coloured by chemically distinct molecules, side view. This structure contains: <ul class='image_legend_ul'><li class='image_legend_li'>1 copy of Fatty acid synthase;</li> <li class='image_legend_li'>1 copy of NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;</li> <li class='image_legend_li'>1 copy of 6-{[(3R)-1-(cyclopropylcarbonyl)pyrrolidin-3-yl]methyl}-5-[4-(1-methyl-1H-indazol-5-yl)phenyl]-4,6-diazaspiro[2.4]hept-4-en-7-one;</li> <li class='image_legend_li'>1 copy of CHLORIDE ION;</li> <li class='image_legend_li'>1 copy of water.</li></ul>}$

$Monomeric assembly 1 of PDB entry 5c37 coloured by chemically distinct molecules, top view. This structure contains: <ul class='image_legend_ul'><li class='image_legend_li'>1 copy of Fatty acid synthase;</li> <li class='image_legend_li'>1 copy of NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;</li> <li class='image_legend_li'>1 copy of 6-{[(3R)-1-(cyclopropylcarbonyl)pyrrolidin-3-yl]methyl}-5-[4-(1-methyl-1H-indazol-5-yl)phenyl]-4,6-diazaspiro[2.4]hept-4-en-7-one;</li> <li class='image_legend_li'>1 copy of CHLORIDE ION;</li> <li class='image_legend_li'>1 copy of water.</li></ul>}$

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Assembly 2 (preferred)

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Assembly Name: Fatty acid synthase
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Multimeric state: monomeric

Accessible surface area: 24675.38 Å²

Buried surface area: 1806.39 Å²

Dissociation area: 121.82 Å²

Dissociation energy (ΔG^diss): -0.14 kcal/mol

Dissociation entropy (TΔS^diss): 1.13 kcal/mol

Symmetry number: 1

PDBe Complex ID: PDB-CPX-155922

$Monomeric assembly 2 of PDB entry 5c37 coloured by chemically distinct molecules, front view. This structure contains: <ul class='image_legend_ul'><li class='image_legend_li'>1 copy of Fatty acid synthase;</li> <li class='image_legend_li'>1 copy of NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;</li> <li class='image_legend_li'>1 copy of 6-{[(3R)-1-(cyclopropylcarbonyl)pyrrolidin-3-yl]methyl}-5-[4-(1-methyl-1H-indazol-5-yl)phenyl]-4,6-diazaspiro[2.4]hept-4-en-7-one;</li> <li class='image_legend_li'>1 copy of CHLORIDE ION;</li> <li class='image_legend_li'>1 copy of GLYCEROL;</li> <li class='image_legend_li'>1 copy of water.</li></ul>}$

$Monomeric assembly 2 of PDB entry 5c37 coloured by chemically distinct molecules, side view. This structure contains: <ul class='image_legend_ul'><li class='image_legend_li'>1 copy of Fatty acid synthase;</li> <li class='image_legend_li'>1 copy of NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;</li> <li class='image_legend_li'>1 copy of 6-{[(3R)-1-(cyclopropylcarbonyl)pyrrolidin-3-yl]methyl}-5-[4-(1-methyl-1H-indazol-5-yl)phenyl]-4,6-diazaspiro[2.4]hept-4-en-7-one;</li> <li class='image_legend_li'>1 copy of CHLORIDE ION;</li> <li class='image_legend_li'>1 copy of GLYCEROL;</li> <li class='image_legend_li'>1 copy of water.</li></ul>}$

$Monomeric assembly 2 of PDB entry 5c37 coloured by chemically distinct molecules, top view. This structure contains: <ul class='image_legend_ul'><li class='image_legend_li'>1 copy of Fatty acid synthase;</li> <li class='image_legend_li'>1 copy of NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;</li> <li class='image_legend_li'>1 copy of 6-{[(3R)-1-(cyclopropylcarbonyl)pyrrolidin-3-yl]methyl}-5-[4-(1-methyl-1H-indazol-5-yl)phenyl]-4,6-diazaspiro[2.4]hept-4-en-7-one;</li> <li class='image_legend_li'>1 copy of CHLORIDE ION;</li> <li class='image_legend_li'>1 copy of GLYCEROL;</li> <li class='image_legend_li'>1 copy of water.</li></ul>}$

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Macromolecules

Fatty acid synthase

Chains: A, C
Length: 664 amino acids
Theoretical weight: 72.05 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:

Canonical: P49327 (Residues: 1108-1523, 1877-2122; Coverage: 26%)

Gene names: FAS, FASN
Pfam:

Methyltransferase domain
Fatty acid synthase, pseudo-KR domain
KR domain

InterPro:

S-adenosyl-L-methionine-dependent methyltransferase superfamily
Methyltransferase type 12
NAD(P)-binding domain superfamily
Polyketide synthase, ketoreductase domain

CATH: NAD(P)-binding Rossmann-like Domain

Fatty acid synthase in PDB entry 5c37, assembly 2, front view.

Fatty acid synthase in PDB entry 5c37, assembly 2, side view.

Fatty acid synthase in PDB entry 5c37, assembly 2, top view.

FASTA Sequence


    >pdb|5c37|A C

EQQVPILEKFCFTPHTEEGCLSERAALQEELQLCKGLVQALQTKVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQVLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLLSPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVAALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESLFSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRPVWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGDLVMNVYRDGAWGAFRHFLLEEDKGGSKTGCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVLSSFVLAEKAAAYRDRD

PDBe-KB: UniProt Coverage View: P49327

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	Chains
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	Secondary structure
	Flexibility predictions
	Early folding residue predictions
	Ligand binding sites
	Sequence conservation
	Variation

UniProt

P49327

Mapping to UniProt FAS_HUMAN

Chains

RSRZ Outlier Chain A

Chain A

RSRZ Outlier Chain B

Chain B

Domains

Residues mapped to CATH domains

Residues mapped to InterPro annotations

Secondary structure

Residues forming Helix

Residues forming Strand

Flexibility predictions

Early folding residue predictions

Ligand binding sites

Residues binding GLYCEROL <img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/GOL_200.svg" />

Residues binding CHLORIDE ION <img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/CL_200.svg" />

Residues binding 6-{[(3R)-1-(cyclopropylcarbonyl)pyrrolidin-3-yl]methyl}-5-[4-(1-methyl-1H-indazol-5-yl)phenyl]-4,6-diazaspiro[2.4]hept-4-en-7-one <img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/4XN_200.svg" />

Residues binding NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE <img src="https://www.ebi.ac.uk/pdbe/static/files/pdbechem_v2/NDP_200.svg" />

Sequence conservation

Amino acid probabilities The amino acid probabilities are calculated using HMM profiles based on multiple sequence alignments. Click to see more details...

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Probability

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Amino acid properties

Aromatic

Polar

Hydrophobic

Negative charge

Proline

Positive charge

Cysteine

Glycine

Variants

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UniProt reviewed

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Observed in PDB

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Molecule details ›

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FASTA (Protein chains A, C)
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Updated mmCIF file
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Structure Factors
SIFTS XML file with residue-level mappings

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Similar 3D structures (PDBeFold)
Similar sequences

BLAST P49327 (UniProt)

Protein Data Bank in Europe

Structure of the beta-ketoacyl reductase domain of human fatty acid synthase bound to a spiro-imidazolone inhibitor

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Assemblies

Assembly 1

Assembly 2 (preferred)

Macromolecules

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PDBe › 5c37 › Structure analysis

Structure of the beta-ketoacyl reductase domain of human fatty acid synthase bound to a spiro-imidazolone inhibitor

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Assemblies

Assembly 1

Assembly 2 (preferred)

Macromolecules

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5c37 › Structure analysis