Protein profile

KP13_03422

putative glutathione S-transferase

Genome: KpKP13

Gene: AHE45799.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GPM8

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Amino acids 201

Annotations 4

Features 17

PDB binders 4

Druggability 0.559

Overview

Basic information about this protein and its source genome.

Accession: KP13_03422
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE45799.1
Status: annotated
Amino acids: 201
Structure source: AlphaFold + ColabFold

GO:0004364 Catalysis of the reaction: RX + glutathione = an S-substituted glutathione + a halide anion + H+. GO:0016034 Catalysis of the reaction: 4-maleylacetoacetate = 4-fumarylacetoacetate. GO:0006749 The chemical reactions and pathways involving glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins; it has a specific role in the reduction of hydrogen peroxide (H2O2) and oxidized ascorbate, and it participates in the gamma-glutamyl cycle. GO:0006559 The chemical reactions and pathways resulting in the breakdown of L-phenylalanine.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 29.464
Human E-value: 1.09e-06
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Unknown
ColabFold pLDDT: 97.12

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 0.559

Structure A0A0H3GPM8

Pocket Pocket 1

P2Rank 0.584

Structure A0A0H3GPM8

Pocket Pocket 1

ColabFold model

FPocket 0.341 · Pocket 2

P2Rank 0.525 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 20 / 4744 genomes with a hit

Normalized 0.004

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

GO:0004364 Catalysis of the reaction: RX + glutathione = an S-substituted glutathione + a halide anion + H+.
GO:0016034 Catalysis of the reaction: 4-maleylacetoacetate = 4-fumarylacetoacetate.
GO:0006749 The chemical reactions and pathways involving glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins; it has a specific role in the reduction of hydrogen peroxide (H2O2) and oxidized ascorbate, and it participates in the gamma-glutamyl cycle.
GO:0006559 The chemical reactions and pathways resulting in the breakdown of L-phenylalanine.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
1	76	Gene3D	G3DSA:3.40.30.10	Glutaredoxin
1	85	SUPERFAMILY	SSF52833	Thioredoxin-like
1	85	InterPro	IPR036249	Thioredoxin-like superfamily
1	71	CDD	cd00570	GST_N_family
23	26	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
15	22	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
1	78	ProSiteProfiles	PS50404	Soluble glutathione S-transferase N-terminal domain profile.
1	78	InterPro	IPR004045	Glutathione S-transferase, N-terminal
80	201	Gene3D	G3DSA:1.20.1050.10	-
1	198	PANTHER	PTHR42673	MALEYLACETOACETATE ISOMERASE
1	26	Phobius	SIGNAL_PEPTIDE	Signal peptide region
3	75	Pfam	PF13417	Glutathione S-transferase, N-terminal domain
3	75	InterPro	IPR004045	Glutathione S-transferase, N-terminal
79	198	SUPERFAMILY	SSF47616	GST C-terminal domain-like
79	198	InterPro	IPR036282	Glutathione S-transferase, C-terminal domain superfamily
1	14	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
27	201	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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_A0A0H3GPM8	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_03422	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				0.559
4				0.184
10				0.003
2				0.0

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	12.88	0.584
2	3.0	0.079
3	2.0	0.036

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
2				0.341
4				0.072
15				0.004
7				0.0

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	11.37	0.525
2	2.51	0.057
3	2.14	0.041

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.

54 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
GSF	4MK3	Q1LJ46	339.3 Da LogP -2.91 TPSA 196.1	1 viol.	✓ Clean	`C(CC(=O)N[C@@H](C[S@@](=O)O)C(=O)NCC(=O)O)[C@@H…`
GSH	3M0F	Q4KDJ6	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`C(CC(=O)N[C@@H](CS)C(=O)NCC(=O)O)[C@@H](C(=O)O)N`
GTS	4JED	B1M0X3	355.3 Da LogP -3.25 TPSA 213.2	1 viol.	✓ Clean	`C(CC(=O)N[C@@H](CS(=O)(=O)O)C(=O)NCC(=O)O)[C@@H…`
GTX	1GWC	O04941	392.5 Da LogP -0.54 TPSA 160.4	✓ Ro5	✓ Clean	`CCCCCCSC[C@@H](C(=O)NCC(=O)O)NC(=O)CC[C@@H](C(=…`

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
ZINC1616627	1.000	355.3 Da LogP -3.25 TPSA 213.2	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS(=O)(=O)O)C(=O)NCC(=O)O)…`
ZINC3830891	1.000	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC3830892	1.000	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC3830893	1.000	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC3830894	1.000	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC5828410	0.821	306.3 Da LogP -2.81 TPSA 164.6	1 viol.	✓ Clean	`NC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@H](N)C(=O)O`
ZINC13549503	0.780	321.4 Da LogP -2.12 TPSA 147.8	✓ Ro5	✓ Clean	`COC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O`
ZINC4096455	0.775	321.4 Da LogP -1.82 TPSA 158.8	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCCC(=O)O)C(=O)O`
ZINC2554974	0.750	289.3 Da LogP -1.73 TPSA 158.8	✓ Ro5	✓ Clean	`CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC3870040	0.750	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS)C(=O)O)C(=O)O`
ZINC3870041	0.750	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CS)C(=O)O)C(=O)O`
ZINC3870042	0.750	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS)C(=O)O)C(=O)O`
ZINC3870043	0.750	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS)C(=O)O)C(=O)O`
ZINC3778474	0.727	349.4 Da LogP -1.34 TPSA 147.8	✓ Ro5	✓ Clean	`CC(C)OC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@H](N)C(=O…`
ZINC3778476	0.727	335.4 Da LogP -1.73 TPSA 147.8	✓ Ro5	✓ Clean	`CCOC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@H](N)C(=O)O`
ZINC5497203	0.727	335.4 Da LogP -1.73 TPSA 147.8	✓ Ro5	✓ Clean	`CCOC(=O)CNC(=O)[C@@H](CS)NC(=O)CC[C@H](N)C(=O)O`
ZINC5497237	0.727	335.4 Da LogP -1.73 TPSA 147.8	✓ Ro5	✓ Clean	`CCOC(=O)CNC(=O)[C@@H](CS)NC(=O)CC[C@@H](N)C(=O)O`
ZINC5497239	0.727	335.4 Da LogP -1.73 TPSA 147.8	✓ Ro5	✓ Clean	`CCOC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@@H](N)C(=O)O`
ZINC1532230	0.714	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4556979	0.714	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4556980	0.714	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4556981	0.714	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC1616624	0.698	355.3 Da LogP -3.25 TPSA 213.2	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS(=O)(=O)O)C(=O)NCC(=O)…`
ZINC1616625	0.698	355.3 Da LogP -3.25 TPSA 213.2	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CS(=O)(=O)O)C(=O)NCC(=O)O…`
ZINC1616626	0.698	355.3 Da LogP -3.25 TPSA 213.2	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS(=O)(=O)O)C(=O)NCC(=O)O…`
ZINC12496578	0.675	275.3 Da LogP -2.12 TPSA 158.8	✓ Ro5	✓ Clean	`C[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC13522300	0.667	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=…`
ZINC31350707	0.667	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC…`
ZINC31350710	0.667	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(…`
ZINC31350713	0.667	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(…`
ZINC3872731	0.667	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CSN=O)C(=O)NCC(=O)O)C(=O…`
ZINC3872732	0.667	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CSN=O)C(=O)NCC(=O)O)C(=O)O`
ZINC3872733	0.667	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CSN=O)C(=O)NCC(=O)O)C(=O)O`
ZINC3872734	0.667	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CSN=O)C(=O)NCC(=O)O)C(=O)O`
ZINC4544082	0.667	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4544083	0.667	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4544084	0.667	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4544085	0.667	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC13451235	0.652	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS[C@H](CC(=O)O)C(=O)O)C…`
ZINC145953214	0.652	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](O)CSC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O…`
ZINC145953600	0.652	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](O)CSC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)…`
ZINC14966489	0.652	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS[C@@H](CC(=O)O)C(=O)O)C…`
ZINC14966492	0.652	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS[C@@H](CC(=O)O)C(=O)O)C(…`
ZINC201224060	0.652	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](O)CSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)…`
ZINC253638410	0.652	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS[C@H](CC(=O)O)C(=O)O)C(=…`
ZINC253638411	0.652	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS[C@H](CC(=O)O)C(=O)O)C(…`
ZINC3920510	0.652	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS[C@@H](CC(=O)O)C(=O)O)…`
ZINC77300920	0.652	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](O)CSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)N…`
ZINC13507523	0.643	303.3 Da LogP -1.48 TPSA 158.8	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4899752	0.641	235.3 Da LogP -2.44 TPSA 121.5	✓ Ro5	✓ Clean	`NCC(=O)N[C@@H](CS)C(=O)NCC(=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.