Protein profile

PA4225

pyochelin synthetase

Genome: NC_002516.2

Gene: PA4225 pchF Structure source: AlphaFold UniProt Q9HWG4

Export view

Amino acids 1809

Annotations 10

Features 57

PDB binders 6

Druggability 0.607

Overview

Basic information about this protein and its source genome.

Accession: PA4225
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4225 pchF
Status: annotated
Amino acids: 1809
Structure source: AlphaFold

6.2.1.69

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0016874 Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient. GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate). GO:0043041 Activation of an amino acid for incorporation into a peptide by a nonribosomal process. GO:0072330 The chemical reactions and pathways resulting in the formation of monocarboxylic acids, any organic acid containing one carboxyl (-COOH) group. 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 (%): 44.444
Human E-value: 2.04e-07
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Unknown

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 0.607

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MSLGELLETCRSRRIELWSEAGRLRYRAPQGALDAGLAERLRAEREALLEHLEGGPGWRAEPDMAHQRFPLTPVQAAYVLGRQAAFDYGGNACQLYAEYDWPADTDPARLEAAWNAMVERHPMLRAVIEDNAWQRVLPEVPWQRLTVHACAGLDEAAFQAHLERVRERLDHACAALDQWPVLRPELSIGRDACVLHCSVDFTLVDYASLQLLLGEWRRRYLDPQWTAEPLEATFRDYVGVEQRRRQSPAWQRDRDWWLARLDALPGRPDLPLRVQPDTRSTRFRHFHARLDEAAWQALGARAGEHGLSAAGVALAAFAETIGRWSQAPAFCLNLTVLNRPPLHPQLAQVLGDFTALSLLAVDSRHGDSFVERARRIGEQMFDDLDHPTFSGVDLLRELARRRGRGADLMPVVFTSGIGSVQRLLGDGEAPRAPRYMISQTPQVWLDCQVTDQFGGLEIGWDVRLGLFPEGQAEAMFDDFVGLLRRLAQSPRAWTDGDATEPVEAPPQALPGSARSIAAGFAERALLTPDATAIHDAAGSYSYRQVAQHASALRRVLEAHGAGRGRRVAVMLPKSAAQLVAVIGILQAGAAYVPVDIRQPPLRRQAILASAEVVALVCLESDVPDVGCACVAIDRLAADSAWPPPPAAEVAADDLAYVIYTSGSTGTPKGVMLSHAAVSNTLLDINQRYGVDANDRVLGLAELSFDLSVYDFFGATAAGAQVVLPDPARGSDPSHWAELLERHAITLWNSVPAQGQMLIDYLESEPQRHLPGPRCVLWSGDWIPVSLPTRWWRRWPDSALFSLGGATEAAIWSIEQPIRPQHTELASIPYGRALRGQSVEVLDARGRRCPPGVRGEIHIGGVGLALGYAGDPQRTAERFVRHPDGRRLYRTGDLGRYLADGSIEFLGREDDQVKIRGHRIELAELDAALCAHPQVNLAATVVLGETHERSLASFVTLHAPVEAGEDPRTALDAVRQRAAQALRRDWGSEEGIAAAVAALDRACLASLAAWLAGSGLFASATPLDLATLCQRLGIAEARQRLLRHWLRQLEEGGYLRAEGEGWLGCAERPAQSPEDAWTAFAGCAPAALWPAELVAYLRDSAQSLGEQLAGRISPAALMFPQGSARIAEAMYSQGLHAQALHEAMAEAIAAIVERQPQRRWRLLELGAGTAAASRTVIARLAPLVQRGAEVDYLFTDVSSYFLAAARERFADQPWVRFGRFDMNGDLLDQGVAPHSVDILLSSGALNNALDTPALLAGLRELLSADAWLVIQELTREHNEISVSQSLMMENPRDLRDERRQLFVHTGQWLEWLAAQGGDLACGVVPPGSALDLLGYDVLLARCKTDRARLEPAELLAFVEARVPRYMLPAQLRVLERLPVTGNGKIDRKALTGFARQPQADLRHGVAQAPADELENALLALWREVLDNPSLGVEQDFFGAGGDSLLIAQLIARLRERLESARRHPFDRLLRWALSQPTPRGLAERLRSAPEEGRGPALAAARGVAPAPAGMSRAPLAEGAVALDPLVRLVPGEGVPRVLVHEGLGTLLPYRPLLRALGEGRPLLGLAVHDSDAYLAIPAEHLNACLGRRYAEALHRAGLREVDLLGYCSGGLVALETAKSLVQRGVRVRQLDIVSSYRIPYRVDDERLLLFSFAATLGLDTAALGFPAPERLGQAVQAALAQTPERLVAEALAGLPGLADLVALRGRVLQAASGSADAVSVERDTLYRLFCHSVRASQAEAPEPYVGALRLFVPDAGNPLVPRYAEALETQWRAAALGACGIHEVPGGHFDCLGEALAQSLSKPMPEEASR

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

6.2.1.69

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0016874 Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient.
GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate).
GO:0043041 Activation of an amino acid for incorporation into a peptide by a nonribosomal process.
GO:0072330 The chemical reactions and pathways resulting in the formation of monocarboxylic acids, any organic acid containing one carboxyl (-COOH) group.
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:0009403 The chemical reactions and pathways resulting in the formation of toxin, a poisonous compound (typically a protein) that is produced by cells or organisms and that can cause disease when introduced into the body or tissues of an organism.
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.

57 records

Show feature table

Start	End	DB	Term	Name
514	908	FunFam	G3DSA:3.40.50.12780:FF:000012	Non-ribosomal peptide synthetase
5	53	Pfam	PF18563	TubC N-terminal docking domain
5	53	InterPro	IPR041464	TubC, N-terminal docking domain
1584	1797	Pfam	PF00975	Thioesterase domain
1584	1797	InterPro	IPR001031	Thioesterase
909	999	Gene3D	G3DSA:3.30.300.30	-
909	999	InterPro	IPR045851	AMP-binding enzyme, C-terminal domain superfamily
63	241	FunFam	G3DSA:3.30.559.10:FF:000023	Non-ribosomal peptide synthetase
1415	1458	Pfam	PF00550	Phosphopantetheine attachment site
1415	1458	InterPro	IPR009081	Phosphopantetheine binding ACP domain
1400	1490	Gene3D	G3DSA:1.10.1200.10	-
1400	1490	InterPro	IPR036736	ACP-like superfamily
1437	1452	ProSitePatterns	PS00012	Phosphopantetheine attachment site.
1437	1452	InterPro	IPR006162	Phosphopantetheine attachment site
247	1494	PANTHER	PTHR45527	NONRIBOSOMAL PEPTIDE SYNTHETASE
520	915	Pfam	PF00501	AMP-binding enzyme
520	915	InterPro	IPR000873	AMP-dependent synthetase/ligase domain
1401	1491	FunFam	G3DSA:1.10.1200.10:FF:000016	Non-ribosomal peptide synthase
1162	1267	Pfam	PF08242	Methyltransferase domain
1162	1267	InterPro	IPR013217	Methyltransferase type 12
1407	1484	SUPERFAMILY	SSF47336	ACP-like
1407	1484	InterPro	IPR036736	ACP-like superfamily
1317	1399	Gene3D	G3DSA:3.30.300.30	-
1317	1399	InterPro	IPR045851	AMP-binding enzyme, C-terminal domain superfamily
64	242	Gene3D	G3DSA:3.30.559.10	-
64	242	InterPro	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily
250	492	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases
528	1010	CDD	cd12114	A_NRPS_TlmIV_like
1407	1488	ProSiteProfiles	PS50075	Carrier protein (CP) domain profile.
1407	1488	InterPro	IPR009081	Phosphopantetheine binding ACP domain
1114	1316	Gene3D	G3DSA:3.40.50.150	Vaccinia Virus protein VP39
1114	1316	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
515	907	Gene3D	G3DSA:3.40.50.12780	-
515	907	InterPro	IPR042099	ANL, N-terminal domain
249	493	FunFam	G3DSA:3.30.559.30:FF:000006	Yersiniabactin polyketide/non-ribosomal peptide synthetase
664	672	PRINTS	PR00154	AMP-binding signature
664	672	InterPro	IPR020459	AMP-binding
652	663	PRINTS	PR00154	AMP-binding signature
652	663	InterPro	IPR020459	AMP-binding
69	490	CDD	cd19535	Cyc_NRPS
541	938	NCBIfam	TIGR01733	amino acid adenylation domain
541	938	InterPro	IPR010071	Amino acid adenylation domain
65	262	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases
248	494	Gene3D	G3DSA:3.30.559.30	Nonribosomal peptide synthetase, condensation domain
1520	1798	SUPERFAMILY	SSF53474	alpha/beta-Hydrolases
1520	1798	InterPro	IPR029058	Alpha/Beta hydrolase fold
657	668	ProSitePatterns	PS00455	Putative AMP-binding domain signature.
657	668	InterPro	IPR020845	AMP-binding, conserved site
1524	1807	Gene3D	G3DSA:3.40.50.1820	alpha/beta hydrolase
1524	1807	InterPro	IPR029058	Alpha/Beta hydrolase fold
69	490	Pfam	PF00668	Condensation domain
69	490	InterPro	IPR001242	Condensation domain
1133	1315	SUPERFAMILY	SSF53335	S-adenosyl-L-methionine-dependent methyltransferases
1133	1315	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
506	1425	SUPERFAMILY	SSF56801	Acetyl-CoA synthetase-like
2	54	Gene3D	G3DSA:1.10.10.1830	-
2	54	InterPro	IPR044894	TubC, N-terminal docking domain superfamily

3D Structure

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

Loading 3D structure...

Legend High Medium Low

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 PA4225	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
3				0.607
4				0.587
1				0.509

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.

14 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
AKR	6LTA	A0A077JG85	72.1 Da LogP 0.26 TPSA 37.3	✓ Ro5	✓ Clean	`C=CC(=O)O`
ANP	6LTB	A0A077JG85	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
B6G	5WMM	Q333U7	432.3 Da LogP -1.37 TPSA 218.2	1 viol.	✓ Clean	`CC(C)[C@@H](C(=O)OP(=O)(O)O[C@H]1[C@H]([C@H]([C…`
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…`
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`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
5CA	A0A2S9PH42	7.40	449.5 Da LogP -3.34 TPSA 217.8	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC8586021	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC2027654	0.531	264.4 Da LogP 0.84 TPSA 75.3	✓ Ro5	✓ Clean	`CC(=O)NCCSC(=O)SCCNC(C)=O`
ZINC12501123	0.516	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC4228234	0.516	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC79671662	0.516	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC79671663	0.516	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC1575002	0.515	292.4 Da LogP -0.22 TPSA 92.3	✓ Ro5	✓ Clean	`CC(=O)NCCSC(=O)C(=O)SCCNC(C)=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.