Protein profile

PA3327

non-ribosomal peptide synthetase

Genome: NC_002516.2

Gene: PA3327 Structure source: AlphaFold UniProt Q9HYR8
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Amino acids 2352
Annotations 9
Features 79
PDB binders 13
Druggability 0.726

Overview

Basic information about this protein and its source genome.

Accession
PA3327
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3327
Status
annotated
Amino acids
2352
Structure source
AlphaFold
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate). GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. GO:0043041 Activation of an amino acid for incorporation into a peptide by a nonribosomal process. GO:0044550 The chemical reactions and pathways resulting in the formation of secondary metabolites, the compounds that are not necessarily required for growth and maintenance of cells, and are often unique to a taxon.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
43.333
Human E-value
1.64e-11
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.726
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MVRFARLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFEARHVDLRADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRTHHIVSDAWGLQLFLSRVRAGYLGELGEPQAQMPTASLLAQLETDDYSGSEQYRGDRAYFAEALEGLEPALFTRRRPAGLRRTARHRLTLERTLLDAIRDRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREATRTLLRHQKMPLGDLLRGASPLFDTTLSYMRWPAAQAIPNASVETVAQTHAHDPDALAIWVSEFDGHSDAQVDFEYACDVFDADFPMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLPTLFAEQVARTPQRTALLEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDERAATLGESLGETRVLHLERLPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGDAVRLVNLYGPTEATVDVSDHECASDNPTRVPIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLPAPPEQVAAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRIRAAAQRRGLGFELADLMRNPTVAGLAERLVRPLAERSYQPFELVSEVDKPRLEGLEDAFPTSRLSLGLLFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGASEPLQLVHTQARSEPLILDLRGNPEAGTVLDEHIRQRRFHRYSLQQPGLFLFAAFVREDGLDLVFSFHHAILDGWSVANLIVALVAAYRGEPLPGPAPALACHVREELAALASPAAVGYWTGLLEGARMTRLDGFGAHEPQAAQGPASHREALPDGLLERLKATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRPELPDADRMVGLFLNTVPVRSEIAGCSWIEVADALFRQERDGHAHRRYPLSAIQQIVGDELSSAFNYVNLHVLEPLWQLRDFRVWEETNFALLVNVIATPSDGMYLRIDSDGRGISRSQAALIGATFVELLWRLADHPDEAADFAFLAPRRDAASQPEPLVDVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQAERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRALPLEHGTNIEYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERLRERSAVRAFDPLVPIRAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGSTPLAVLEDIAASYLAAIRRVQPEGPYYLGGWSFGGFVAYEMARQLRALDPQAVAQLIVLDSITVDRNHAGSASDEALLLFFYWELVWFERSDKEVEPLPEGASLEQKLDHIVERAIEAGVLPAGTPRATVQRLYELFRASWQALIGYRPEVSDQDMTLLRADGPLPLALKPMHDAAGTHYGDPKNGWQHWTSGRLDVIDVPGDHLVLMKEPYVETVAAEIAALLEPSTSSERTRP

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

9 GO

Gene Ontology (GO)

9
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate).
  • GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
  • GO:0043041 Activation of an amino acid for incorporation into a peptide by a nonribosomal process.
  • GO:0044550 The chemical reactions and pathways resulting in the formation of secondary metabolites, the compounds that are not necessarily required for growth and maintenance of cells, and are often unique to a taxon.
  • GO:0044281 The chemical reactions and pathways involving small molecules, any low molecular weight, monomeric, non-encoded molecule.
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
  • GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.

Sequence Features

Domain/signature hits from InterPro and related databases.

79 records
Show feature table
Start End DB Term Name
455 764 Gene3D G3DSA:3.40.50.980 -
765 842 Gene3D G3DSA:2.30.38.10 Luciferase; Domain 3
604 764 FunFam G3DSA:3.40.50.980:FF:000002 Enterobactin synthetase component F
2066 2346 FunFam G3DSA:3.40.50.1820:FF:000439 Non-ribosomal peptide synthetase OfaC
474 603 FunFam G3DSA:3.40.50.980:FF:000001 Non-ribosomal peptide synthetase
950 1024 ProSiteProfiles PS50075 Carrier protein (CP) domain profile.
950 1024 InterPro IPR009081 Phosphopantetheine binding ACP domain
980 995 ProSitePatterns PS00012 Phosphopantetheine attachment site.
980 995 InterPro IPR006162 Phosphopantetheine attachment site
1871 1977 Gene3D G3DSA:3.30.300.30 -
1871 1977 InterPro IPR045851 AMP-binding enzyme, C-terminal domain superfamily
846 947 FunFam G3DSA:3.30.300.30:FF:000010 Enterobactin synthetase component F
459 939 CDD cd05930 A_NRPS
1475 1870 Gene3D G3DSA:3.40.50.12780 -
1475 1870 InterPro IPR042099 ANL, N-terminal domain
1042 1227 Gene3D G3DSA:3.30.559.10 -
1042 1227 InterPro IPR023213 Chloramphenicol acetyltransferase-like domain superfamily
5 189 Gene3D G3DSA:3.30.559.10 -
5 189 InterPro IPR023213 Chloramphenicol acetyltransferase-like domain superfamily
947 1025 Gene3D G3DSA:1.10.1200.10 -
947 1025 InterPro IPR036736 ACP-like superfamily
474 606 Gene3D G3DSA:3.40.50.980 -
451 852 Pfam PF00501 AMP-binding enzyme
451 852 InterPro IPR000873 AMP-dependent synthetase/ligase domain
1481 1877 Pfam PF00501 AMP-binding enzyme
1481 1877 InterPro IPR000873 AMP-dependent synthetase/ligase domain
186 436 SUPERFAMILY SSF52777 CoA-dependent acyltransferases
1471 2001 SUPERFAMILY SSF56801 Acetyl-CoA synthetase-like
1481 1970 CDD cd17651 A_NRPS_VisG_like
1227 1457 SUPERFAMILY SSF52777 CoA-dependent acyltransferases
1228 1468 Gene3D G3DSA:3.30.559.30 Nonribosomal peptide synthetase, condensation domain
190 437 Gene3D G3DSA:3.30.559.30 Nonribosomal peptide synthetase, condensation domain
947 1022 FunFam G3DSA:1.10.1200.10:FF:000005 Nonribosomal peptide synthetase 1
9 167 SUPERFAMILY SSF52777 CoA-dependent acyltransferases
445 845 FunFam G3DSA:3.40.50.12780:FF:000012 Non-ribosomal peptide synthetase
766 842 FunFam G3DSA:2.30.38.10:FF:000001 Non-ribosomal peptide synthetase PvdI
2056 2341 SUPERFAMILY SSF53474 alpha/beta-Hydrolases
2056 2341 InterPro IPR029058 Alpha/Beta hydrolase fold
6 415 CDD cd19533 starter-C_NRPS
1980 2064 Gene3D G3DSA:1.10.1200.10 -
1980 2064 InterPro IPR036736 ACP-like superfamily
1984 2059 ProSiteProfiles PS50075 Carrier protein (CP) domain profile.
1984 2059 InterPro IPR009081 Phosphopantetheine binding ACP domain
1982 2056 SUPERFAMILY SSF47336 ACP-like
1982 2056 InterPro IPR036736 ACP-like superfamily
1045 1238 SUPERFAMILY SSF52777 CoA-dependent acyltransferases
2078 2338 Pfam PF00975 Thioesterase domain
2078 2338 InterPro IPR001031 Thioesterase
949 1020 SUPERFAMILY SSF47336 ACP-like
949 1020 InterPro IPR036736 ACP-like superfamily
1617 1628 ProSitePatterns PS00455 Putative AMP-binding domain signature.
1617 1628 InterPro IPR020845 AMP-binding, conserved site
956 1024 SMART SM00823 Phosphopantetheine attachment site
956 1024 InterPro IPR020806 Polyketide synthase, phosphopantetheine-binding domain
1987 2059 SMART SM00823 Phosphopantetheine attachment site
1987 2059 InterPro IPR020806 Polyketide synthase, phosphopantetheine-binding domain
413 969 SUPERFAMILY SSF56801 Acetyl-CoA synthetase-like
958 1020 Pfam PF00550 Phosphopantetheine attachment site
958 1020 InterPro IPR009081 Phosphopantetheine binding ACP domain
1992 2055 Pfam PF00550 Phosphopantetheine attachment site
1992 2055 InterPro IPR009081 Phosphopantetheine binding ACP domain
473 876 NCBIfam TIGR01733 amino acid adenylation domain
473 876 InterPro IPR010071 Amino acid adenylation domain
1502 1894 NCBIfam TIGR01733 amino acid adenylation domain
1502 1894 InterPro IPR010071 Amino acid adenylation domain
2067 2346 Gene3D G3DSA:3.40.50.1820 alpha/beta hydrolase
2067 2346 InterPro IPR029058 Alpha/Beta hydrolase fold
1042 1227 FunFam G3DSA:3.30.559.10:FF:000082 Probable non-ribosomal peptide synthetase
864 933 Pfam PF13193 AMP-binding enzyme C-terminal domain
864 933 InterPro IPR025110 AMP-binding enzyme, C-terminal domain
591 602 ProSitePatterns PS00455 Putative AMP-binding domain signature.
591 602 InterPro IPR020845 AMP-binding, conserved site
8 232 PANTHER PTHR45527 NONRIBOSOMAL PEPTIDE SYNTHETASE
847 946 Gene3D G3DSA:3.30.300.30 -
847 946 InterPro IPR045851 AMP-binding enzyme, C-terminal domain superfamily
7 430 Pfam PF00668 Condensation domain
7 430 InterPro IPR001242 Condensation domain
1057 1457 Pfam PF00668 Condensation domain
1057 1457 InterPro IPR001242 Condensation domain

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA3327
AlphaFold — — full sequence — Viewing
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
13 0.726
5 0.341
1 0.233

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

63 records

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
5S4
5ES8
Q70LM7 440.4 Da LogP -1.80 TPSA 200.3 1 viol. ✓ Clean CC(C)[C@@H](C(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C)(C…
9EF
6MFX
Q70LM7 383.3 Da LogP -1.76 TPSA 174.3 1 viol. ✓ Clean CC(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP(=O)(O)…
APC
5ES7
Q70LM7 505.2 Da LogP -1.52 TPSA 269.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
CO8
7C1R
E5ATN9 893.7 Da LogP 1.03 TPSA 363.6 3 viol. ✓ Clean CCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…
DG9
6MG0
Q70LM7 785.8 Da LogP -2.85 TPSA 336.7 3 viol. ✓ Clean CC(C)[C@H]([C@H](CS(=O)(=O)NC[C@@H]1[C@H]([C@H]…
FGU
7C1S
E5ATN9 232.3 Da LogP 0.76 TPSA 72.2 ✓ Ro5 ✓ Clean CC(C)C[C@@H](C(=O)SCCNC(=O)C)N
FLC
6P1J
A0A0B5H0S3 189.1 Da LogP -5.25 TPSA 140.6 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
FON
5ES7
Q70LM7 473.4 Da LogP -0.73 TPSA 219.8 1 viol. ✓ Clean c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC[C@@H]2…
JQG
6MFW
Q70LM7 468.4 Da LogP -1.84 TPSA 200.2 1 viol. ✓ Clean CC(C)[C@@H](C(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C)(C…
KH4
4PWV
F2YRY5 452.4 Da LogP -0.60 TPSA 190.9 1 viol. ✓ Clean CC(C)(COP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCSC(=O)c…
KIV
6ULZ
Q70LM7 116.1 Da LogP 0.30 TPSA 54.4 ✓ Ro5 ✓ Clean CC(C)C(=O)C(=O)O
MUY
6OJD
Q5J1Q6 419.4 Da LogP 1.02 TPSA 153.2 ✓ Ro5 ✓ Clean CP(=O)([C@@H](c1ccc(cc1)O)N2C[C@@H](C2=O)NC(=O)…
PNS
5ES9
Q70LM7 358.4 Da LogP -0.96 TPSA 145.2 1 viol. ✓ Clean CC(C)(COP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCS)O

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.