Protein profile

KP13_03500

Protein moaE

Genome: KpKP13

Gene: AHE45876.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GPH4

Export view

Amino acids 254

Annotations 1

Features 26

PDB binders 9

Druggability 0.043

Overview

Basic information about this protein and its source genome.

Accession: KP13_03500
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE45876.1
Status: annotated
Amino acids: 254
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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 39.785
Human E-value: 5.7e-11
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 97.37

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 0.043

Structure A0A0H3GPH4

Pocket Pocket 2

P2Rank 0.932

Structure A0A0H3GPH4

Pocket Pocket 1

ColabFold model

FPocket 0.268 · Pocket 19

P2Rank 0.947 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 14 / 4744 genomes with a hit

Normalized 0.003

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

26 records

Show feature table

Start	End	DB	Term	Name
142	161	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
142	161	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
163	180	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
163	180	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
70	81	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
70	81	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
38	55	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
38	55	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
207	227	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
207	227	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
116	132	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
116	132	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
2	246	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
2	246	InterPro	IPR036291	NAD(P)-binding domain superfamily
2	177	SMART	SM00822	This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
129	157	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
129	157	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
142	161	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
70	81	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
122	130	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
122	130	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
14	240	CDD	cd05233	SDR_c
1	249	Gene3D	G3DSA:3.40.50.720	-
1	248	FunFam	G3DSA:3.40.50.720:FF:000084	Short-chain dehydrogenase reductase
2	244	PANTHER	PTHR42879	3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE
8	243	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase

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 + 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_A0A0H3GPH4	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_03500	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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				22.49	0.881
2				5.35	0.253

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
19				0.268

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				20.84	0.863
2				6.19	0.308

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.

59 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
3HR	3VDR	D0VWQ0	104.1 Da LogP -0.16 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](CC(=O)O)O`
A6O	6IHH	C0IR58	314.4 Da LogP 3.93 TPSA 46.5	✓ Ro5	✓ Clean	`CC[C@]1([C@H](CCC1=O)O)C/C=C/2\CCCc3c2ccc(c3)OC`
AAE	6ZZQ	A0A1E3M3N6	102.1 Da LogP 0.05 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CC(=O)O`
DXX	3W8D	D0VWQ0	118.1 Da LogP -0.21 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C(=O)O)C(=O)O`
EMO	2RH4	P16544	270.2 Da LogP 1.89 TPSA 94.8	✓ Ro5	Alert	`Cc1cc2c(c(c1)O)C(=O)c3c(cc(cc3O)O)C2=O`
ISZ	1XR3	P16544	135.1 Da LogP 1.25 TPSA 66.2	✓ Ro5	Alert	`[H]/N=N/C(=O)c1ccncc1`
MLA	3W8F	D0VWQ0	104.1 Da LogP -0.45 TPSA 74.6	✓ Ro5	✓ Clean	`C(C(=O)O)C(=O)O`
QT8	6ZZS	A0A1E3M3N6	116.1 Da LogP 0.44 TPSA 54.4	✓ Ro5	✓ Clean	`CCC(=O)CC(=O)O`
TAM	4BMN	C0IR58	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`

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
ZINC3824868	1.000	270.2 Da LogP 1.89 TPSA 94.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC4095655	0.735	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1cc(O)cc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC1532902	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC3978794	0.697	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1cc(O)c2c(c1)C(=O)c1cc(C)cc(O)c1C2=O`
ZINC3861630	0.688	254.2 Da LogP 2.18 TPSA 74.6	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cccc(O)c1C2=O`
ZINC1845623	0.673	312.4 Da LogP 4.13 TPSA 43.4	✓ Ro5	✓ Clean	`CCC1(C/C=C2\CCCc3cc(OC)ccc32)C(=O)CCC1=O`
ZINC1845624	0.673	312.4 Da LogP 4.13 TPSA 43.4	✓ Ro5	✓ Clean	`CCC1(C/C=C2/CCCc3cc(OC)ccc32)C(=O)CCC1=O`
ZINC14760847	0.667	286.2 Da LogP 1.59 TPSA 115.1	✓ Ro5	Alert	`Cc1cc2c(c(O)c1O)C(=O)c1c(O)cc(O)cc1C2=O`
ZINC5277130	0.656	238.2 Da LogP 2.48 TPSA 54.4	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1ccccc1C2=O`
ZINC3593496	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC4098655	0.629	304.7 Da LogP 2.54 TPSA 94.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)c(Cl)c(O)c1C2=O`
ZINC14686440	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC2575038	0.625	205.3 Da LogP 0.00 TPSA 86.7	✓ Ro5	✓ Clean	`NC(CCCO)(CCCO)CCCO`
ZINC5461939	0.618	286.2 Da LogP 1.59 TPSA 115.1	✓ Ro5	Alert	`Cc1cc(O)c2c(c1O)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC14814143	0.595	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1c(O)ccc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC13481200	0.594	240.2 Da LogP 1.87 TPSA 74.6	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c(O)cc(O)cc21`
ZINC3977762	0.588	300.2 Da LogP 1.28 TPSA 132.1	✓ Ro5	Alert	`O=C(O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC5812872	0.588	286.2 Da LogP 1.07 TPSA 115.1	✓ Ro5	Alert	`O=C1c2cc(O)cc(O)c2C(=O)c2c(O)cc(CO)cc21`
ZINC6070245	0.588	256.3 Da LogP 2.25 TPSA 77.8	✓ Ro5	✓ Clean	`Cc1cc(O)c2c(c1)Cc1cc(O)cc(O)c1C2=O`
ZINC14760863	0.579	300.3 Da LogP 1.90 TPSA 104.1	✓ Ro5	Alert	`COc1c(O)c(C)cc2c1C(=O)c1c(O)cc(O)cc1C2=O`
ZINC6070262	0.579	314.2 Da LogP 1.59 TPSA 132.1	✓ Ro5	Alert	`Cc1cc2c(c(O)c1C(=O)O)C(=O)c1c(O)cc(O)cc1C2=O`
ZINC13398039	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC14819806	0.568	314.3 Da LogP 1.50 TPSA 115.1	✓ Ro5	Alert	`C[C@@H](O)Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC14819808	0.568	314.3 Da LogP 1.50 TPSA 115.1	✓ Ro5	Alert	`C[C@H](O)Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC31163880	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@@H](O)[C@@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc…`
ZINC31163884	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@H](O)[C@@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(…`
ZINC31163888	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@@H](O)[C@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(…`
ZINC31163892	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@H](O)[C@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(O…`
ZINC13334425	0.564	268.3 Da LogP 2.48 TPSA 63.6	✓ Ro5	Alert	`COc1cccc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC13546016	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@@H](C)CC(=O)O[C@@H](C)CC(=O)O`
ZINC13546018	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@H](C)CC(=O)O[C@@H](C)CC(=O)O`
ZINC146315135	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315336	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@](O)(CC(=O)O)C(=O)O`
ZINC257400894	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@H](C)CC(=O)O[C@H](C)CC(=O)O`
ZINC257400895	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@@H](C)CC(=O)O[C@H](C)CC(=O)O`
ZINC14760819	0.553	300.3 Da LogP 1.90 TPSA 104.1	✓ Ro5	Alert	`COc1cc(O)c2c(c1O)C(=O)c1cc(C)cc(O)c1C2=O`
ZINC5412537	0.553	316.3 Da LogP 1.60 TPSA 124.3	✓ Ro5	Alert	`COc1c(O)c(O)c2c(c1O)C(=O)c1cc(C)cc(O)c1C2=O`
ZINC20111521	0.550	327.3 Da LogP 1.95 TPSA 98.1	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)c(CN(C)C)c(O)c1C2=O`
ZINC1662285	0.544	284.4 Da LogP 3.35 TPSA 43.4	✓ Ro5	✓ Clean	`COc1ccc2c(c1)CC/C2=C\CC1(C)C(=O)CCC1=O`
ZINC17380200	0.544	284.4 Da LogP 3.35 TPSA 43.4	✓ Ro5	✓ Clean	`COc1ccc2c(c1)CC/C2=C/CC1(C)C(=O)CCC1=O`
ZINC77257242	0.538	316.3 Da LogP 1.43 TPSA 124.3	✓ Ro5	Alert	`COCc1c(O)cc2c(c1O)C(=O)c1c(O)cc(O)cc1C2=O`
ZINC1637808	0.528	267.1 Da LogP 2.36 TPSA 54.4	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)C=C(Br)C2=O`
ZINC13398014	0.522	220.2 Da LogP -1.07 TPSA 110.1	✓ Ro5	✓ Clean	`COC(=O)CC(O)(CC(=O)OC)C(=O)O`
ZINC14811261	0.512	300.3 Da LogP 1.37 TPSA 104.1	✓ Ro5	Alert	`COc1cc(CO)cc2c1C(=O)c1c(O)cc(O)cc1C2=O`
ZINC4098672	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@@H]3O[C@H](CO…`

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.