Protein profile

VK055_3380

6-phospho-alpha-glucosidase

Genome: KpATCC43816

Gene: aglB AIK81937.1 Structure source: Experimental + ColabFold UniProt Q9AGA6

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Amino acids 440

Annotations 8

Features 36

PDB binders 2

Druggability 0.681

Overview

Basic information about this protein and its source genome.

Accession: VK055_3380
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: aglB AIK81937.1
Status: annotated
Amino acids: 440
Structure source: Experimental + ColabFold

3.2.1.122

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:0004553 Catalysis of the hydrolysis of any O-glycosyl bond. GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP. GO:0050081 Catalysis of the reaction: H2O + maltose 6'-phosphate = D-glucose + D-glucose 6-phosphate. GO:0046872 Binding to a metal ion.

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: 95.72

Selected Druggability evidence

PDB experimental structure

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 0.681

Structure 6DUX

Pocket Pocket 1

P2Rank 0.926

Structure 6DUX

Pocket Pocket 1

ColabFold model

FPocket 0.443 · Pocket 4

P2Rank 0.969 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 432 / 4744 genomes with a hit

Normalized 0.091

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)

3.2.1.122

Gene Ontology (GO)

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:0004553 Catalysis of the hydrolysis of any O-glycosyl bond.
GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
GO:0050081 Catalysis of the reaction: H2O + maltose 6'-phosphate = D-glucose + D-glucose 6-phosphate.
GO:0046872 Binding to a metal ion.
GO:0005985 The chemical reactions and pathways involving sucrose, the disaccharide fructofuranosyl-glucopyranoside.

Sequence Features

Domain/signature hits from InterPro and related databases.

36 records

Show feature table

Start	End	DB	Term	Name
6	25	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
167	440	Gene3D	G3DSA:3.90.110.10	-
167	440	InterPro	IPR015955	Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
138	169	ProSitePatterns	PS01324	Glycosyl hydrolases family 4 signature.
138	169	InterPro	IPR019802	Glycoside hydrolase, family 4, conserved site
5	27	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	439	PANTHER	PTHR32092	6-PHOSPHO-BETA-GLUCOSIDASE-RELATED
1	439	InterPro	IPR001088	Glycoside hydrolase, family 4
3	164	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
3	164	InterPro	IPR036291	NAD(P)-binding domain superfamily
1	166	Gene3D	G3DSA:3.40.50.720	-
6	184	Pfam	PF02056	Family 4 glycosyl hydrolase
6	184	InterPro	IPR001088	Glycoside hydrolase, family 4
4	440	CDD	cd05298	GH4_GlvA_pagL_like
26	440	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
1	5	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	166	FunFam	G3DSA:3.40.50.720:FF:000295	6-phospho-alpha-glucosidase
168	439	SUPERFAMILY	SSF56327	LDH C-terminal domain-like
168	439	InterPro	IPR015955	Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
138	155	PRINTS	PR00732	Glycosyl hydrolase family 4 signature
138	155	InterPro	IPR001088	Glycoside hydrolase, family 4
191	203	PRINTS	PR00732	Glycosyl hydrolase family 4 signature
191	203	InterPro	IPR001088	Glycoside hydrolase, family 4
5	20	PRINTS	PR00732	Glycosyl hydrolase family 4 signature
5	20	InterPro	IPR001088	Glycoside hydrolase, family 4
74	90	PRINTS	PR00732	Glycosyl hydrolase family 4 signature
74	90	InterPro	IPR001088	Glycoside hydrolase, family 4
95	108	PRINTS	PR00732	Glycosyl hydrolase family 4 signature
95	108	InterPro	IPR001088	Glycoside hydrolase, family 4
164	175	PRINTS	PR00732	Glycosyl hydrolase family 4 signature
164	175	InterPro	IPR001088	Glycoside hydrolase, family 4
109	129	PRINTS	PR00732	Glycosyl hydrolase family 4 signature
109	129	InterPro	IPR001088	Glycoside hydrolase, family 4
167	440	FunFam	G3DSA:3.90.110.10:FF:000010	6-phospho-alpha-glucosidase
195	415	Pfam	PF11975	Family 4 glycosyl hydrolase C-terminal domain
195	415	InterPro	IPR022616	Glycosyl hydrolase, family 4, C-terminal

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

2 + 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 6DUX	X-ray	2.25 Å	A,B	99.8% 2-440	PDBe RCSB PDBj File	Loaded
PDB 6DVV	X-ray	2.25 Å	A,B	99.8% 2-440	PDBe RCSB PDBj File	Viewing
ColabFold VK055_3380	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				0.542
49				0.201

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	28.51	0.925
2	12.05	0.637
3	2.79	0.086
4	2.47	0.068
5	2.03	0.044

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
4				0.443

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	34.86	0.951
2	2.29	0.058
3	1.86	0.036

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.

52 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.

Ligand	Source crystal	MW · LogP · TPSA	Lipinski	PAINS	SMILES
LMR	6DUX 2.25 Å Open crystal	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)O)C(=O)O`

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
G6P	1U8X	P54716	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O)OP…`

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
ZINC100351935	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@H](O)[C@H](O)[C@@…`
ZINC1529564	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@H](O)[C@H](O)[C@…`
ZINC1532533	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC1532857	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C…`
ZINC3581460	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C…`
ZINC38276879	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC38276880	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@H…`
ZINC3869397	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H](O)[C…`
ZINC3875374	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@…`
ZINC3875375	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@…`
ZINC4095545	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@…`
ZINC4095546	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H…`
ZINC4096188	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@@H](O)[C@…`
ZINC8551507	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC12504154	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@@H]1O`
ZINC1532546	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H]1O`
ZINC4096190	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H]1O`
ZINC4228241	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H]1O`
ZINC4521831	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H]1O`
ZINC13516910	0.733	244.1 Da LogP -2.42 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC2562340	0.733	244.1 Da LogP -2.42 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC4097102	0.719	259.2 Da LogP -3.14 TPSA 162.7	1 viol.	✓ Clean	`N[C@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC4097103	0.719	259.2 Da LogP -3.14 TPSA 162.7	1 viol.	✓ Clean	`N[C@H]1[C@@H](O)O[C@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC12502703	0.667	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](OP(=O)(O)O)[C@H](O)[C@…`
ZINC4095589	0.667	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](OP(=O)(O)O)[C@H](O)[C@@…`
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`
ZINC15298193	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@H…`
ZINC1933262384	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@H…`
ZINC1933262385	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@H…`
ZINC1933262386	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@H]…`
ZINC1933262387	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@H]…`
ZINC256073272	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@H…`
ZINC256073273	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@…`
ZINC256073274	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@H…`
ZINC256073275	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@…`
ZINC4228300	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@H]2O[C@H](CO)[C@@H]…`
ZINC56870785	0.656	228.1 Da LogP -1.40 TPSA 116.5	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](O)[C@H]1O`
ZINC13522068	0.636	310.1 Da LogP -2.35 TPSA 183.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](OP(=O)(O)O)[C@H](O)[C@@…`
ZINC3870205	0.636	310.1 Da LogP -2.35 TPSA 183.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](OP(=O)(O)O)[C@@H](O)[C…`
ZINC4095560	0.636	310.1 Da LogP -2.35 TPSA 183.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](OP(=O)(O)O)[C@H](O)[C@…`
ZINC13513381	0.622	301.2 Da LogP -2.12 TPSA 169.3	1 viol.	✓ Clean	`C/C(O)=N/[C@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@H]…`
ZINC30725927	0.622	301.2 Da LogP -2.12 TPSA 169.3	1 viol.	✓ Clean	`C/C(O)=N/[C@H]1[C@@H](O)O[C@H](COP(=O)(O)O)[C@H…`
ZINC1530414	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@@H](O)O[C@@H](COP(=O)(O)O)[C@H…`
ZINC245204467	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@H]1[C@H](O)[C@@H](O)[C@@H](COP(=O)(O)…`
ZINC245204468	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@H]1[C@H](O)[C@H](O)[C@@H](COP(=O)(O)O…`
ZINC30725207	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC4096363	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@@H](O)O[C@H](COP(=O)(O)O)[C@@H…`
ZINC4097101	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@@H](…`

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.