Protein profile

PA0962

DNA-binding stress protein

Genome: NC_002516.2

Gene: PA0962 Structure source: Experimental + AlphaFold UniProt Q9I4Z7

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Amino acids 156

Annotations 5

Features 22

PDB binders 3

Druggability 0.914

Overview

Basic information about this protein and its source genome.

Accession: PA0962
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA0962
Status: annotated
Amino acids: 156
Structure source: Experimental + AlphaFold

GO:1990084 A protein complex that negatively regulates strand-opening at the origin of replication, thereby interfering with replication initiation. This complex is thought to be involved in the regulation of replication under oxidative stress conditions. In E. coli, this complex is composed of DnaA and Dps. GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). GO:0008199 Binding to a ferric iron ion, Fe(III). GO:0016722 Catalysis of an oxidation-reduction in which the oxidation state of metal ion is altered. GO:0032297 Any process that stops, prevents, or reduces the frequency, rate or extent of initiation of DNA-dependent DNA replication.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
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 0.914

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

GO:1990084 A protein complex that negatively regulates strand-opening at the origin of replication, thereby interfering with replication initiation. This complex is thought to be involved in the regulation of replication under oxidative stress conditions. In E. coli, this complex is composed of DnaA and Dps.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0008199 Binding to a ferric iron ion, Fe(III).
GO:0016722 Catalysis of an oxidation-reduction in which the oxidation state of metal ion is altered.
GO:0032297 Any process that stops, prevents, or reduces the frequency, rate or extent of initiation of DNA-dependent DNA replication.

Sequence Features

Domain/signature hits from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
37	53	ProSitePatterns	PS00818	Dps protein family signature 1.
37	53	InterPro	IPR023188	DNA-binding protein Dps, conserved site
4	155	SUPERFAMILY	SSF47240	Ferritin-like
4	155	InterPro	IPR009078	Ferritin-like superfamily
1	156	PIRSF	PIRSF005900	Dps
1	156	InterPro	IPR002177	DNA-binding protein Dps
1	155	Gene3D	G3DSA:1.20.1260.10	-
1	155	InterPro	IPR012347	Ferritin-like
63	77	ProSitePatterns	PS00819	Dps protein family signature 2.
63	77	InterPro	IPR023188	DNA-binding protein Dps, conserved site
17	154	CDD	cd01043	DPS
17	154	InterPro	IPR002177	DNA-binding protein Dps
17	155	Pfam	PF00210	Ferritin-like domain
17	155	InterPro	IPR008331	Ferritin/DPS protein domain
3	155	PANTHER	PTHR42932	GENERAL STRESS PROTEIN 20U
3	155	InterPro	IPR002177	DNA-binding protein Dps
37	53	PRINTS	PR01346	Helicobacter neutrophil-activating protein A family signature
37	53	InterPro	IPR002177	DNA-binding protein Dps
132	150	PRINTS	PR01346	Helicobacter neutrophil-activating protein A family signature
132	150	InterPro	IPR002177	DNA-binding protein Dps
61	77	PRINTS	PR01346	Helicobacter neutrophil-activating protein A family signature
61	77	InterPro	IPR002177	DNA-binding protein Dps

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

5 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
PDB 8FF9	X-ray	1.70 Å	A,B,C,D,E,F,G,H,I,J,K,L	100.0% 1-156	PDBe RCSB PDBj File	Viewing
PDB 8FFC	X-ray	1.85 Å	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P	100.0% 1-156	PDBe RCSB PDBj File	Loaded
PDB 8FFA	X-ray	2.15 Å	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P	100.0% 1-156	PDBe RCSB PDBj File	Loaded
PDB 8FFD	X-ray	2.20 Å	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P	100.0% 1-156	PDBe RCSB PDBj File	Loaded
PDB 8FFB	X-ray	2.25 Å	A,B,C,D,E,F,G,H,I,J,K,L	100.0% 1-156	PDBe RCSB PDBj File	Loaded
AlphaFold PA0962	AlphaFold	—	—	full sequence	—	Loaded

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				0.914

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				3.21	0.11

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				0.683
3				0.311

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.

37 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
FEO	1N1Q	P83695	127.7 Da LogP -0.07 TPSA 9.2	✓ Ro5	✓ Clean	`O([Fe])[Fe]`
OFE	2YJJ	Q1X6M4	71.8 Da LogP -0.12 TPSA 17.1	✓ Ro5	✓ Clean	`O=[Fe]`
SIN	2XGW	Q99YU7	118.1 Da LogP -0.06 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=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).

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
ZINC1529497	0.615	230.3 Da LogP 3.06 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCC(=O)O`
ZINC1531045	0.615	202.2 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)O`
ZINC1593115	0.615	216.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCC(=O)O`
ZINC1700020	0.615	244.3 Da LogP 3.45 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCC(=O)O`
ZINC3860440	0.615	258.4 Da LogP 3.84 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(=O)O`
ZINC3861298	0.615	286.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCC(=O)O`
ZINC5113062	0.615	272.4 Da LogP 4.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCC(=O)O`
ZINC1572706	0.563	260.2 Da LogP -1.05 TPSA 132.8	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)NCCNC(=O)CCC(=O)O`
ZINC1703342	0.533	202.2 Da LogP 1.07 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)CCCC(=O)O`
ZINC1728397	0.533	233.2 Da LogP -0.29 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)CCN(CCC(=O)O)CCC(=O)O`
ZINC2508031	0.533	230.3 Da LogP 1.85 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCC(=O)CCCCC(=O)O`
ZINC2517013	0.533	250.2 Da LogP 0.89 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)CCP(CCC(=O)O)CCC(=O)O`
ZINC1697439	0.529	219.5 Da LogP 1.79 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)C(Cl)(Cl)Cl`
ZINC35465466	0.529	244.3 Da LogP 2.24 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCC(=O)CCC(=O)O`
ZINC39208104	0.529	262.2 Da LogP -0.20 TPSA 127.2	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)OCCOC(=O)CCC(=O)O`
ZINC145743383	0.500	266.2 Da LogP 0.77 TPSA 129.0	✓ Ro5	✓ Clean	`O=C(O)CCP(=O)(CCC(=O)O)CCC(=O)O`
ZINC1542984448	0.500	470.5 Da LogP 0.07 TPSA 148.4	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCOCCOCCOCCC(=O)O`
ZINC1586444	0.500	210.2 Da LogP -0.65 TPSA 108.7	✓ Ro5	✓ Clean	`O=C(O)CCS(=O)(=O)CCC(=O)O`
ZINC1753095	0.500	238.3 Da LogP 1.40 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCSCCSCCC(=O)O`
ZINC22028383	0.500	204.2 Da LogP -0.88 TPSA 98.7	✓ Ro5	✓ Clean	`O=C(O)CCNCCNCCC(=O)O`
ZINC22576322	0.500	348.4 Da LogP -0.51 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CCN(CCC(=O)O)CCN(CCC(=O)O)CCC(=O)O`
ZINC26897400	0.500	286.4 Da LogP 3.41 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCCC(=O)O`
ZINC3074813	0.500	258.3 Da LogP 2.63 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCCCC(=O)O`
ZINC34423725	0.500	342.5 Da LogP 4.97 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC35977596	0.500	294.3 Da LogP 0.00 TPSA 111.5	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCC(=O)O`
ZINC38682833	0.500	286.3 Da LogP -0.61 TPSA 115.2	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)N1CCN(C(=O)CCC(=O)O)CC1`
ZINC39383060	0.500	206.2 Da LogP -0.03 TPSA 93.1	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCC(=O)O`
ZINC39427081	0.500	250.2 Da LogP -0.01 TPSA 102.3	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCC(=O)O`
ZINC4181831	0.500	232.2 Da LogP -0.01 TPSA 129.0	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)C(CC(=O)O)CC(=O)O`
ZINC4822898	0.500	272.3 Da LogP 3.02 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCC(=O)O`
ZINC4822900	0.500	300.4 Da LogP 3.80 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCC(=O)O`
ZINC71257127	0.500	426.5 Da LogP 0.05 TPSA 139.2	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCOCCOCCC(=O)O`
ZINC71257128	0.500	338.4 Da LogP 0.02 TPSA 120.8	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCC(=O)O`
ZINC79016464	0.500	382.4 Da LogP 0.04 TPSA 130.0	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCOCCC(=O)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.