Protein profile

PA0317

hypothetical protein

Genome: NC_002516.2

Gene: PA0317 Structure source: AlphaFold UniProt Q9I6H4

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Amino acids 464

Annotations 8

Features 24

PDB binders 13

Druggability 0.603

Overview

Basic information about this protein and its source genome.

Accession: PA0317
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA0317
Status: annotated
Amino acids: 464
Structure source: AlphaFold

1.1.99.39

GO:0051990 Catalysis of the reaction: (R)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor. GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. GO:0046872 Binding to a metal ion. GO:0006564 The chemical reactions and pathways resulting in the formation of L-serine. GO:0022904 A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient. 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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 40.833
Human E-value: 3.7400000000000006e-27
Gut microbiome off-target: hit
Essential (DEG): Y
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 0.603

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1.1.99.39

Gene Ontology (GO)

GO:0051990 Catalysis of the reaction: (R)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor.
GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
GO:0046872 Binding to a metal ion.
GO:0006564 The chemical reactions and pathways resulting in the formation of L-serine.
GO:0022904 A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
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:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
1	92	FunFam	G3DSA:3.30.43.10:FF:000020	FAD-binding oxidoreductase
37	216	ProSiteProfiles	PS51387	PCMH-type FAD-binding domain profile.
37	216	InterPro	IPR016166	FAD-binding domain, PCMH-type
422	461	Gene3D	G3DSA:1.10.45.10	-
422	461	InterPro	IPR016171	Vanillyl-alcohol oxidase, C-terminal subdomain 2
4	462	PANTHER	PTHR43716	D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL
95	214	Gene3D	G3DSA:3.30.465.10	-
95	214	InterPro	IPR016169	FAD-binding, type PCMH, subdomain 2
1	92	Gene3D	G3DSA:3.30.43.10	-
1	92	InterPro	IPR016167	FAD-binding, type PCMH, subdomain 1
336	421	FunFam	G3DSA:3.30.70.2740:FF:000005	FAD-binding oxidoreductase
95	214	FunFam	G3DSA:3.30.465.10:FF:000025	FAD-binding oxidoreductase
217	333	Gene3D	G3DSA:3.30.70.2190	-
217	461	Pfam	PF02913	FAD linked oxidases, C-terminal domain
217	461	InterPro	IPR004113	FAD-binding oxidoreductase/transferase, type 4, C-terminal
4	217	SUPERFAMILY	SSF56176	FAD-binding/transporter-associated domain-like
4	217	InterPro	IPR036318	FAD-binding, type PCMH-like superfamily
336	421	Gene3D	G3DSA:3.30.70.2740	-
41	179	Pfam	PF01565	FAD binding domain
41	179	InterPro	IPR006094	FAD linked oxidase, N-terminal
222	463	SUPERFAMILY	SSF55103	FAD-linked oxidases, C-terminal domain
222	463	InterPro	IPR016164	FAD-linked oxidase-like, C-terminal
422	462	FunFam	G3DSA:1.10.45.10:FF:000001	D-lactate dehydrogenase mitochondrial
217	333	FunFam	G3DSA:3.30.70.2190:FF:000002	FAD-binding oxidoreductase

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 PA0317	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				0.603

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.

64 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
1DO	4BC7	P97275	186.3 Da LogP 3.90 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO`
2HG	6LPP	Q8N465	148.1 Da LogP -0.70 TPSA 94.8	✓ Ro5	✓ Clean	`C(CC(=O)O)[C@H](C(=O)O)O`
AKG	6LPX	Q8N465	146.1 Da LogP -0.50 TPSA 91.7	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)C(=O)O`
AWB	5AE3	P97275	548.6 Da LogP 3.48 TPSA 157.3	1 viol.	✓ Clean	`CCCCCC[C@@H]1[C@H]([C@@H](OC(=O)[C@H]([C@H](OC1…`
B2Z	5AE1	P97275	341.4 Da LogP 3.37 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)N[C@H](C)c1ccc2c(c1)NC(=O)N2)c3cc…`
F6T	6GOU	P97275	345.3 Da LogP 2.94 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)NCc1ccc2c(c1)NC(=O)N2)c3c(cccc3F)F`
FYC	5AE2	P97275	325.3 Da LogP 2.71 TPSA 77.8	✓ Ro5	✓ Clean	`C/C(=C\c1ccccc1F)/C(=O)NCc2ccc3c(c2)NC(=O)N3`
KQS	5ADZ	P97275	327.4 Da LogP 2.81 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)NCc1ccc2c(c1)NC(=O)N2)c3ccccc3F`
LAC	6LPT	Q8N465	90.1 Da LogP -0.55 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)O`
MLT	6LPQ	Q8N465	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
PCR	1DIQ	P09788	108.1 Da LogP 1.70 TPSA 20.2	✓ Ro5	✓ Clean	`Cc1ccc(cc1)O`
PL3	2UUU	O96759	242.4 Da LogP 5.46 TPSA 20.2	1 viol.	✓ Clean	`CCCCCCCCCCCCCCCCO`
S2G	6LPU	Q8N465	148.1 Da LogP -0.70 TPSA 94.8	✓ Ro5	✓ Clean	`C(CC(=O)O)[C@@H](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
CHEMBL4563407	O00116	—	345.3 Da LogP 2.94 TPSA 77.8	✓ Ro5	✓ Clean	`CC(CC(=O)NCc1ccc2[nH]c(=O)[nH]c2c1)c1c(F)cccc1F`

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
ZINC1644076	1.000	214.4 Da LogP 4.68 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCO`
ZINC1680803	1.000	200.4 Da LogP 4.29 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCO`
ZINC12505585	0.684	200.2 Da LogP 3.49 TPSA 29.5	✓ Ro5	✓ Clean	`Cc1ccc(Oc2ccc(O)cc2)cc1`
ZINC2149802	0.684	210.4 Da LogP 3.90 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCC#CCCCCCCO`
ZINC254518779	0.684	212.3 Da LogP 4.12 TPSA 45.0	✓ Ro5	Alert	`Cc1ccc(N=Nc2ccc(O)cc2)cc1`
ZINC2555300	0.684	238.4 Da LogP 4.68 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCC#CCCCCCCCCO`
ZINC2579260	0.684	238.4 Da LogP 4.68 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCC#CCCCCCCO`
ZINC4948010	0.684	212.3 Da LogP 4.12 TPSA 45.0	✓ Ro5	Alert	`Cc1ccc(/N=N/c2ccc(O)cc2)cc1`
ZINC59724910	0.684	212.4 Da LogP 4.46 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCC/C=C/CCCCO`
ZINC59724924	0.684	212.4 Da LogP 4.46 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCO`
ZINC59724927	0.684	212.4 Da LogP 4.46 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCO`
ZINC95831576	0.684	230.4 Da LogP 3.92 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCCCO`
ZINC1857579176	0.679	345.3 Da LogP 3.36 TPSA 78.0	✓ Ro5	✓ Clean	`C[C@H](CC(=O)NCc1ccc2nc(O)[nH]c2c1)c1c(F)cccc1F`
ZINC1857606065	0.679	345.3 Da LogP 3.36 TPSA 78.0	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)NCc1ccc2nc(O)[nH]c2c1)c1c(F)cccc1F`
ZINC71773889	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@H](O)C(=O)O`
ZINC71773890	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC71773891	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC1587596	0.650	212.2 Da LogP 2.93 TPSA 37.3	✓ Ro5	✓ Clean	`Cc1ccc(C(=O)c2ccc(O)cc2)cc1`
ZINC59996054	0.650	214.3 Da LogP 2.78 TPSA 40.5	✓ Ro5	✓ Clean	`Cc1ccc([C@H](O)c2ccc(O)cc2)cc1`
ZINC59996055	0.650	214.3 Da LogP 2.78 TPSA 40.5	✓ Ro5	✓ Clean	`Cc1ccc([C@@H](O)c2ccc(O)cc2)cc1`
ZINC100244447	0.619	276.5 Da LogP 4.04 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCC[S@@](=O)CCCCCCCO`
ZINC100244449	0.619	276.5 Da LogP 4.04 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCC[S@](=O)CCCCCCCO`
ZINC1593169	0.619	248.3 Da LogP 2.53 TPSA 54.4	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)c2ccc(O)cc2)cc1`
ZINC5746567	0.619	213.3 Da LogP 2.75 TPSA 46.2	✓ Ro5	✓ Clean	`Cc1ccc([C@H](N)c2ccc(O)cc2)cc1`
ZINC5746613	0.619	213.3 Da LogP 2.75 TPSA 46.2	✓ Ro5	✓ Clean	`Cc1ccc([C@@H](N)c2ccc(O)cc2)cc1`
ZINC98008412	0.619	250.4 Da LogP 2.53 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCS(=O)(=O)CCCCO`
ZINC98008413	0.619	234.4 Da LogP 2.87 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCC[S@@](=O)CCCCO`
ZINC98008414	0.619	234.4 Da LogP 2.87 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCC[S@](=O)CCCCO`
ZINC14771652	0.615	216.4 Da LogP 3.26 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCCCCCCCO`
ZINC15269439	0.615	272.5 Da LogP 4.82 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCCCCCCCCCCCO`
ZINC1574339	0.615	202.3 Da LogP 2.87 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCCCCCCO`
ZINC4202510	0.615	230.4 Da LogP 3.65 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCCCCCCCCO`
ZINC4521552	0.615	258.4 Da LogP 4.43 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCCCCCCCCCCO`
ZINC4600152	0.615	244.4 Da LogP 4.04 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCCCCCCCCCO`
ZINC97106986	0.604	303.3 Da LogP 2.06 TPSA 77.8	✓ Ro5	✓ Clean	`O=C(NCc1ccc2[nH]c(=O)[nH]c2c1)c1cccc(F)c1F`
ZINC100245871	0.600	232.4 Da LogP 4.24 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCCSCCCO`
ZINC13558894	0.600	262.3 Da LogP 4.43 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(-c2ccc(-c3ccc(O)cc3)cc2)cc1`
ZINC1682375	0.600	215.4 Da LogP 3.05 TPSA 23.5	✓ Ro5	✓ Clean	`CCCCN(CCCC)CCCCCO`
ZINC2009358	0.600	212.4 Da LogP 4.46 TPSA 20.2	✓ Ro5	✓ Clean	`CCCC/C=C/CCCCCCCCO`
ZINC2555306	0.600	238.4 Da LogP 4.68 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCC#CCCCCCCCCCCO`
ZINC2555345	0.600	210.4 Da LogP 3.90 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCC#CCCCCCCCCO`
ZINC4409966	0.600	257.5 Da LogP 4.22 TPSA 23.5	✓ Ro5	✓ Clean	`CCCCN(CCCC)CCCCCCCCO`
ZINC4409972	0.600	271.5 Da LogP 4.61 TPSA 23.5	✓ Ro5	✓ Clean	`CCCCN(CCCC)CCCCCCCCCO`
ZINC4528894	0.600	212.4 Da LogP 4.46 TPSA 20.2	✓ Ro5	✓ Clean	`CCCC/C=C\CCCCCCCCO`
ZINC59545536	0.600	258.4 Da LogP 4.70 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCOCCCO`
ZINC74998281	0.600	315.3 Da LogP 1.69 TPSA 87.0	✓ Ro5	✓ Clean	`O=C(COc1ccccc1F)NCc1ccc2[nH]c(=O)[nH]c2c1`
ZINC104156515	0.591	283.5 Da LogP 4.80 TPSA 42.2	✓ Ro5	✓ Clean	`CCCCCCCC[C@H]1N[C@H]1CCCCCCCCO`
ZINC104156519	0.591	283.5 Da LogP 4.80 TPSA 42.2	✓ Ro5	✓ Clean	`CCCCCCCC[C@@H]1N[C@H]1CCCCCCCCO`
ZINC104156523	0.591	283.5 Da LogP 4.80 TPSA 42.2	✓ Ro5	✓ Clean	`CCCCCCCC[C@H]1N[C@@H]1CCCCCCCCO`
ZINC104156528	0.591	283.5 Da LogP 4.80 TPSA 42.2	✓ Ro5	✓ Clean	`CCCCCCCC[C@@H]1N[C@@H]1CCCCCCCCO`

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.