Protein profile

KP13_01925

putative oxidoreductase

Genome: KpKP13

Gene: AHE46367.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GRN6

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Amino acids 677

Annotations 2

Features 21

PDB binders 6

Druggability 0.856

Overview

Basic information about this protein and its source genome.

Accession: KP13_01925
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE46367.1
Status: annotated
Amino acids: 677
Structure source: AlphaFold + ColabFold

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. GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 95.36

Selected Druggability evidence

AlphaFold / UniProt model

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 0.856

Structure A0A0H3GRN6

Pocket Pocket 1

P2Rank 0.98

Structure A0A0H3GRN6

Pocket Pocket 1

ColabFold model

FPocket 0.71 · Pocket 13

P2Rank 0.976 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 152 / 4744 genomes with a hit

Normalized 0.032

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 GO

Gene Ontology (GO)

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.
GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.

Sequence Features

Domain/signature hits from InterPro and related databases.

21 records

Show feature table

Start	End	DB	Term	Name
8	335	CDD	cd02803	OYE_like_FMN_family
7	336	Pfam	PF00724	NADH:flavin oxidoreductase / NADH oxidase family
7	336	InterPro	IPR001155	NADH:flavin oxidoreductase/NADH oxidase, N-terminal
481	610	Gene3D	G3DSA:3.50.50.60	-
481	610	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1	382	Gene3D	G3DSA:3.20.20.70	Aldolase class I
1	382	InterPro	IPR013785	Aldolase-type TIM barrel
385	619	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
385	619	InterPro	IPR023753	FAD/NAD(P)-binding domain
385	407	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
418	433	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
469	487	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
519	537	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
386	405	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
602	618	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
341	547	SUPERFAMILY	SSF51971	Nucleotide-binding domain
473	637	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
473	637	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
386	652	Gene3D	G3DSA:3.40.50.720	-
1	542	PANTHER	PTHR42917	2,4-DIENOYL-COA REDUCTASE
3	355	SUPERFAMILY	SSF51395	FMN-linked oxidoreductases

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 + 2

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GRN6	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_01925	ColabFold	—	—	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				0.856
37				0.317

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	Score	Probability
1	26.84	0.917
2	18.87	0.831
3	12.69	0.659
4	4.39	0.184
5	1.92	0.039

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				0.71

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	Score	Probability
1	25.55	0.907
2	18.0	0.813
3	10.94	0.587
4	3.93	0.155
5	2.8	0.086

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.

56 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
BTB	3GR8	Q5KXG9	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
HBA	1Z42	P54550	122.1 Da LogP 1.20 TPSA 37.3	✓ Ro5	✓ Clean	`c1cc(ccc1C=O)O`
J5H	6QKR	E1YD54	921.7 Da LogP 1.13 TPSA 363.6	3 viol.	✓ Clean	`CC(C)(COP(=O)(O)OP(=O)(O)OC[C@@H]1[C@H]([C@H]([…`
MDE	1PS9	P42593	994.9 Da LogP 0.91 TPSA 382.6	3 viol.	✓ Clean	`CCCCC[C@@H](C\C=C\C(=O)SCCNC(=O)CCNC(C(=O)C(C)(…`
NPO	1Z44	P54550	139.1 Da LogP 1.30 TPSA 63.4	✓ Ro5	✓ Clean	`c1cc(ccc1[N+](=O)[O-])O`
TXD	3KRZ	B0KAH1	667.5 Da LogP -3.30 TPSA 317.6	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`

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
ZINC1615342	1.000	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN(CCO)C(CO)(CO)CO`
ZINC1507107	0.857	215.2 Da LogP 2.97 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2ccc(O)cc2)cc1`
ZINC100009138	0.750	243.2 Da LogP 3.72 TPSA 88.1	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(/N=N\c2ccc(O)cc2)cc1`
ZINC100009140	0.750	243.2 Da LogP 3.72 TPSA 88.1	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(/N=N/c2ccc(O)cc2)cc1`
ZINC13836765	0.750	247.3 Da LogP 3.45 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Sc2ccc(O)cc2)cc1`
ZINC1562026	0.750	229.2 Da LogP 2.89 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Cc2ccc(O)cc2)cc1`
ZINC189331	0.750	279.3 Da LogP 2.13 TPSA 97.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(S(=O)(=O)c2ccc(O)cc2)cc1`
ZINC1911545360	0.750	241.2 Da LogP 3.47 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(C=Cc2ccc(O)cc2)cc1`
ZINC225426	0.750	241.2 Da LogP 3.47 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(/C=C/c2ccc(O)cc2)cc1`
ZINC254392989	0.750	243.2 Da LogP 3.72 TPSA 88.1	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(N=Nc2ccc(O)cc2)cc1`
ZINC33246164	0.750	241.2 Da LogP 3.47 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(/C=C\c2ccc(O)cc2)cc1`
ZINC370769	0.750	231.2 Da LogP 3.09 TPSA 72.6	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Oc2ccc(O)cc2)cc1`
ZINC38237571	0.750	243.2 Da LogP 2.53 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(c1ccc(O)cc1)c1ccc([N+](=O)[O-])cc1`
ZINC8419013	0.750	230.2 Da LogP 3.04 TPSA 75.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Nc2ccc(O)cc2)cc1`
ZINC2386334759	0.727	226.2 Da LogP 3.62 TPSA 62.0	✓ Ro5	Alert	`O=Cc1ccc(N=Nc2ccc(O)cc2)cc1`
ZINC8586019	0.681	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC21982756	0.667	299.3 Da LogP 2.63 TPSA 69.9	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(N2CCN(c3ccc(O)cc3)CC2)cc1`
ZINC33835370	0.667	273.2 Da LogP 2.94 TPSA 104.5	✓ Ro5	✓ Clean	`O=C(Nc1ccc(O)cc1)Nc1ccc([N+](=O)[O-])cc1`
ZINC1604377	0.619	320.3 Da LogP 4.84 TPSA 86.3	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2ccc(-c3ccc([N+](=O)[O-])cc…`
ZINC1648209	0.619	244.2 Da LogP 3.17 TPSA 86.3	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2ccc([N+](=O)[O-])cc2)cc1`
ZINC2173334	0.609	300.2 Da LogP 2.57 TPSA 120.4	✓ Ro5	Alert	`O=C(C(=O)c1ccc([N+](=O)[O-])cc1)c1ccc([N+](=O)[…`
ZINC145787882	0.600	259.2 Da LogP 2.52 TPSA 89.7	✓ Ro5	✓ Clean	`O=C(Oc1ccc([N+](=O)[O-])cc1)c1ccc(O)cc1`
ZINC18036964	0.600	242.2 Da LogP 3.05 TPSA 75.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(/C=N/c2ccc(O)cc2)cc1`
ZINC18099346	0.600	242.2 Da LogP 3.05 TPSA 75.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(/N=C/c2ccc(O)cc2)cc1`
ZINC225997	0.600	258.2 Da LogP 2.55 TPSA 92.5	✓ Ro5	✓ Clean	`O=C(Nc1ccc(O)cc1)c1ccc([N+](=O)[O-])cc1`
ZINC36019045	0.600	276.2 Da LogP 2.58 TPSA 126.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O)c(-c2cc([N+](=O)[O-])ccc2O)…`
ZINC369682	0.600	294.3 Da LogP 2.10 TPSA 109.5	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(S(=O)(=O)Nc2ccc(O)cc2)cc1`
ZINC1688116	0.583	272.2 Da LogP 2.73 TPSA 103.3	✓ Ro5	✓ Clean	`O=C(c1ccc([N+](=O)[O-])cc1)c1ccc([N+](=O)[O-])c…`
ZINC5731136	0.581	278.3 Da LogP 2.44 TPSA 92.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc([S@](=O)Nc2ccc(O)cc2)cc1`
ZINC5731137	0.581	278.3 Da LogP 2.44 TPSA 92.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc([S@@](=O)Nc2ccc(O)cc2)cc1`
ZINC114628575	0.579	236.3 Da LogP 3.48 TPSA 34.1	✓ Ro5	✓ Clean	`O=Cc1ccc(/C=C\c2ccc(C=O)cc2)cc1`
ZINC116811203	0.579	286.3 Da LogP 4.65 TPSA 34.1	✓ Ro5	✓ Clean	`O=Cc1ccc(-c2ccc(-c3ccc(C=O)cc3)cc2)cc1`
ZINC13319959	0.579	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C\c2ccc(O)cc2)cc1`
ZINC1510311	0.579	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C/c2ccc(O)cc2)cc1`
ZINC1875408805	0.579	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(C=Cc2ccc(O)cc2)cc1`
ZINC2041311	0.579	210.2 Da LogP 2.98 TPSA 34.1	✓ Ro5	✓ Clean	`O=Cc1ccc(-c2ccc(C=O)cc2)cc1`
ZINC33847575	0.579	236.3 Da LogP 3.48 TPSA 34.1	✓ Ro5	✓ Clean	`O=Cc1ccc(/C=C/c2ccc(C=O)cc2)cc1`
ZINC2539986	0.571	215.2 Da LogP 2.97 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2cccc(O)c2)cc1`
ZINC33427614	0.571	215.2 Da LogP 2.97 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(-c2ccc(O)cc2)c1`
ZINC1511626	0.565	249.0 Da LogP 2.20 TPSA 43.1	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(I)cc1`
ZINC1666827	0.565	202.0 Da LogP 2.36 TPSA 43.1	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Br)cc1`
ZINC1750178	0.563	272.3 Da LogP 2.48 TPSA 92.5	✓ Ro5	✓ Clean	`O=C(Cc1ccc([N+](=O)[O-])cc1)Nc1ccc(O)cc1`
ZINC4616626	0.563	257.2 Da LogP 2.75 TPSA 87.8	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(N/N=C/c2ccc(O)cc2)cc1`
ZINC7718004	0.563	269.3 Da LogP 3.20 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccc([N+](=O)[O-])cc1)c1ccc(O)cc1`
ZINC104058859	0.560	395.3 Da LogP 3.70 TPSA 149.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(C(O)(c2ccc([N+](=O)[O-])cc2)c…`
ZINC2584252	0.560	203.2 Da LogP 0.84 TPSA 97.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(S(=O)(=O)O)cc1`
ZINC1571129	0.542	308.3 Da LogP 2.34 TPSA 120.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(S(=O)(=O)c2ccc([N+](=O)[O-])c…`
ZINC1712904	0.542	276.3 Da LogP 3.65 TPSA 86.3	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Sc2ccc([N+](=O)[O-])cc2)cc1`
ZINC4522652	0.542	259.2 Da LogP 3.25 TPSA 98.3	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Nc2ccc([N+](=O)[O-])cc2)cc1`
ZINC66139588	0.542	379.3 Da LogP 4.59 TPSA 129.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(C(c2ccc([N+](=O)[O-])cc2)c2cc…`

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.