Protein profile

PA4620

hypothetical protein

Genome: NC_002516.2

Gene: PA4620 Structure source: AlphaFold UniProt Q9HVH1

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Amino acids 179

Annotations 5

Features 15

PDB binders 15

Druggability 0.725

Overview

Basic information about this protein and its source genome.

Accession: PA4620
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4620
Status: annotated
Amino acids: 179
Structure source: AlphaFold

GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0046872 Binding to a metal ion. GO:0016903 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor. GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 27.439
Human E-value: 7e-07
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 0.725

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MANRKLQMTLNGQAVGPVEVAEDLPMIDYLHEYQNLTGSRLGCGQGICHACVVIVDNPDGTSEEVRTCITGAHYFDGKKVRTIEGHAQRDENGDIRELNPIQQKFVDQFAFQCSYCAPGFVNAATVLVEKAQRQPIKRSELEQAIEDSLGHHICRCTGYVRYYSATRDVLDELGLVKEA

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0046872 Binding to a metal ion.
GO:0016903 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Sequence Features

Domain/signature hits from InterPro and related databases.

15 records

Show feature table

Start	End	DB	Term	Name
82	166	Pfam	PF01799	[2Fe-2S] binding domain
82	166	InterPro	IPR002888	[2Fe-2S]-binding
94	174	Gene3D	G3DSA:1.10.150.120	-
1	85	FunFam	G3DSA:3.10.20.30:FF:000044	(2Fe-2S)-binding domain-containing protein
99	174	SUPERFAMILY	SSF47741	CO dehydrogenase ISP C-domain like
99	174	InterPro	IPR036884	[2Fe-2S]-binding domain superfamily
4	87	SUPERFAMILY	SSF54292	2Fe-2S ferredoxin-like
4	87	InterPro	IPR036010	2Fe-2S ferredoxin-like superfamily
2	177	PANTHER	PTHR45331	OXIDOREDUCTASE, IRON-SULPHUR BINDING SUBUNIT-RELATED-RELATED
18	63	Pfam	PF00111	2Fe-2S iron-sulfur cluster binding domain
18	63	InterPro	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain
1	85	Gene3D	G3DSA:3.10.20.30	-
1	85	InterPro	IPR012675	Beta-grasp domain superfamily
4	86	ProSiteProfiles	PS51085	2Fe-2S ferredoxin-type iron-sulfur binding domain profile.
4	86	InterPro	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain

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...

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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 PA4620	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
1				0.725

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.

65 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
141	1JRP	O54050	152.1 Da LogP -1.11 TPSA 94.4	✓ Ro5	✓ Clean	`C1=C2C(=NC(=O)NC2=O)NN1`
CUB	1N62	P19921	306.7 Da LogP 1.27 TPSA 32.8	✓ Ro5	✓ Clean	`CCCCN([C@@]12O[Mo+4]1(=O)S2)[Cu+]`
CUM	1N5W	P19921	224.6 Da LogP -0.03 TPSA 37.3	✓ Ro5	✓ Clean	`O[Mo+6](=O)S[Cu+]`
CUN	1N61	P19921	224.6 Da LogP -0.03 TPSA 37.3	✓ Ro5	✓ Clean	`O[Mo+4](=O)S[Cu+]`
FES	1RM6	O33818	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
HHR	2W54	O54050	193.2 Da LogP -1.21 TPSA 117.8	✓ Ro5	✓ Clean	`c1c(nc2c(n1)N=C(NC2=O)N)CO`
HPA	2W3R	O54050	136.1 Da LogP -0.35 TPSA 74.4	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)N=CNC2=O`
MCN	1T3Q	P72223	696.5 Da LogP -1.29 TPSA 319.9	3 viol.	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
MOM	2W3R	O54050	144.9 Da LogP -0.80 TPSA 54.4	✓ Ro5	✓ Clean	`O[Mo](=O)=O`
MOS	1JRO	O54050	161.0 Da LogP 0.14 TPSA 34.1	✓ Ro5	✓ Clean	`O=[Mo](=O)S`
MTE	1JRO	O54050	395.4 Da LogP -0.54 TPSA 171.8	1 viol.	✓ Clean	`C([C@@H]1C(=C([C@H]2[C@@H](O1)NC3=C(N2)C(=O)NC(…`
OMO	1N60	P19921	146.0 Da LogP -1.24 TPSA 57.5	✓ Ro5	✓ Clean	`O[Mo+6](=O)O`
SMO	1T3Q	P72223	160.0 Da LogP 0.41 TPSA 34.1	✓ Ro5	✓ Clean	`O=[Mo](=O)=S`
XAN	2W3S	O54050	152.1 Da LogP -1.06 TPSA 94.4	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)C(=O)NC(=O)N2`
XAX	2W54	O54050	554.4 Da LogP -0.03 TPSA 209.1	3 viol.	✓ Clean	`C([C@@H]1C2=C([C@H]3[C@@H](O1)NC4=C(N3)C(=O)NC(…`

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).

No ChEMBL hits found through similar proteins.

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
ZINC17429362	0.806	207.2 Da LogP -1.17 TPSA 117.8	✓ Ro5	✓ Clean	`Nc1nc2ncc(CCO)nc2c(=O)[nH]1`
ZINC142664839	0.730	211.6 Da LogP 0.03 TPSA 97.5	✓ Ro5	✓ Clean	`Nc1nc2ncc(CCl)nc2c(=O)[nH]1`
ZINC12428336	0.605	253.2 Da LogP -2.32 TPSA 158.2	✓ Ro5	✓ Clean	`Nc1nc2ncc([C@H](O)[C@H](O)CO)nc2c(=O)[nH]1`
ZINC17176122	0.605	253.2 Da LogP -2.32 TPSA 158.2	✓ Ro5	✓ Clean	`Nc1nc2ncc([C@@H](O)[C@@H](O)CO)nc2c(=O)[nH]1`
ZINC17176123	0.605	253.2 Da LogP -2.32 TPSA 158.2	✓ Ro5	✓ Clean	`Nc1nc2ncc([C@H](O)[C@@H](O)CO)nc2c(=O)[nH]1`
ZINC18169010	0.605	253.2 Da LogP -2.32 TPSA 158.2	✓ Ro5	✓ Clean	`Nc1nc2ncc([C@@H](O)[C@H](O)CO)nc2c(=O)[nH]1`
ZINC5127809	0.600	207.1 Da LogP -1.01 TPSA 134.8	✓ Ro5	✓ Clean	`Nc1nc2ncc(C(=O)O)nc2c(=O)[nH]1`
ZINC4706270	0.596	313.3 Da LogP 0.57 TPSA 144.1	✓ Ro5	✓ Clean	`Nc1nc2ncc(COc3ccc(C(=O)O)cc3)nc2c(=O)[nH]1`
ZINC12502055	0.579	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC12502057	0.579	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC12502058	0.579	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13431057	0.579	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13431059	0.579	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC25726736	0.579	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC3861746	0.579	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@@](=O)(O)…`
ZINC53683723	0.579	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC82142138	0.579	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC82142140	0.579	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC104864216	0.573	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@](=O)(O)OP(=O)(O)O)[C…`
ZINC12504412	0.573	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC12504413	0.573	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC12504414	0.573	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431045	0.573	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431047	0.573	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC13548733	0.573	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC33913782	0.573	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC8215624	0.573	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC6628789	0.571	312.3 Da LogP 0.61 TPSA 146.9	✓ Ro5	✓ Clean	`Nc1nc2ncc(CNc3ccc(C(=O)O)cc3)nc2c(=O)[nH]1`
ZINC8627299	0.571	262.0 Da LogP 0.25 TPSA 74.4	✓ Ro5	✓ Clean	`O=c1[nH]cnc2nc(I)[nH]c12`
ZINC8216134	0.564	446.2 Da LogP -2.35 TPSA 238.9	2 viol.	✓ Clean	`NCCO[P@@](=O)(O)O[P@](=O)(O)OC[C@H]1O[C@@H](n2c…`
ZINC8216074	0.556	477.3 Da LogP -2.95 TPSA 253.3	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@](=O)(O)…`
ZINC8551188	0.556	477.3 Da LogP -2.95 TPSA 253.3	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)O…`
ZINC8616322	0.549	326.3 Da LogP 0.65 TPSA 146.9	✓ Ro5	✓ Clean	`Nc1nc2ncc(CCNc3ccc(C(=O)O)cc3)nc2c(=O)[nH]1`
ZINC17129255	0.545	237.2 Da LogP -1.29 TPSA 138.0	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H](O)c1cnc2nc(N)[nH]c(=O)c2n1`
ZINC17129257	0.545	237.2 Da LogP -1.29 TPSA 138.0	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H](O)c1cnc2nc(N)[nH]c(=O)c2n1`
ZINC17129259	0.545	237.2 Da LogP -1.29 TPSA 138.0	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](O)c1cnc2nc(N)[nH]c(=O)c2n1`
ZINC18275062	0.545	237.2 Da LogP -1.29 TPSA 138.0	✓ Ro5	✓ Clean	`C[C@H](O)[C@H](O)c1cnc2nc(N)[nH]c(=O)c2n1`
ZINC101145080	0.537	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC106404522	0.537	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC12660526	0.537	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@H]1…`
ZINC16696677	0.537	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1O…`
ZINC215821427	0.537	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC36382611	0.537	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@H]1…`
ZINC5048329	0.537	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@](=O)(O)OC[C@H]1O…`
ZINC6507065	0.537	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@H]1…`
ZINC9211548	0.537	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1O…`
ZINC96023557	0.537	489.3 Da LogP -1.60 TPSA 212.9	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@H]1…`
ZINC339536	0.535	239.2 Da LogP 0.96 TPSA 97.5	✓ Ro5	✓ Clean	`Nc1nc2ncc(-c3ccccc3)nc2c(=O)[nH]1`
ZINC146373408	0.532	337.2 Da LogP -1.79 TPSA 166.4	✓ Ro5	✓ Clean	`CO[P@](=O)(O)OC[C@@H]1O[C@H](n2ccc(N)nc2=O)[C@H…`
ZINC36471998	0.532	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](COP(=O)(OP(=O)(O)O)OP(=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.