Protein profile

KP13_31943

Asparagine synthetase B glutamine-hydrolyzing

Genome: KpKP13

Gene: asnB AHE45696.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GQ75

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Amino acids 554

Annotations 5

Features 26

PDB binders 8

Druggability 0.995

Overview

Basic information about this protein and its source genome.

Accession: KP13_31943
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: asnB AHE45696.1
Status: annotated
Amino acids: 554
Structure source: AlphaFold + ColabFold

6.3.5.4

GO:0004066 Catalysis of the reaction: ATP + L-aspartate + L-glutamine = AMP + diphosphate + L-asparagine + L-glutamate. GO:0006529 OBSOLETE. The chemical reactions and pathways resulting in the formation of asparagine, 2-amino-3-carbamoylpropanoic acid. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 37.5
Human E-value: 1.28e-102
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 96.23

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 0.995

Structure A0A0H3GQ75

Pocket Pocket 1

P2Rank 0.973

Structure A0A0H3GQ75

Pocket Pocket 1

ColabFold model

FPocket 0.996 · Pocket 1

P2Rank 0.986 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 396 / 4744 genomes with a hit

Normalized 0.083

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

6.3.5.4

Gene Ontology (GO)

GO:0004066 Catalysis of the reaction: ATP + L-aspartate + L-glutamine = AMP + diphosphate + L-asparagine + L-glutamate.
GO:0006529 OBSOLETE. The chemical reactions and pathways resulting in the formation of asparagine, 2-amino-3-carbamoylpropanoic acid.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Sequence Features

Domain/signature hits from InterPro and related databases.

26 records

Show feature table

Start	End	DB	Term	Name
48	166	Pfam	PF13537	Glutamine amidotransferase domain
48	166	InterPro	IPR017932	Glutamine amidotransferase type 2 domain
361	507	PIRSF	PIRSF001589	Asn_synthetase_glu-h
361	507	InterPro	IPR006426	Asparagine synthase, glutamine-hydrolyzing
1	368	PIRSF	PIRSF001589	Asn_synthetase_glu-h
1	368	InterPro	IPR006426	Asparagine synthase, glutamine-hydrolyzing
194	514	FunFam	G3DSA:3.40.50.620:FF:000031	Asparagine synthase B
1	554	PANTHER	PTHR11772	ASPARAGINE SYNTHETASE
2	373	NCBIfam	TIGR01536	asparagine synthase (glutamine-hydrolyzing)
2	373	InterPro	IPR006426	Asparagine synthase, glutamine-hydrolyzing
2	193	CDD	cd00712	AsnB
2	193	InterPro	IPR033738	Asparagine synthase, N-terminal domain
210	479	SUPERFAMILY	SSF52402	Adenine nucleotide alpha hydrolases-like
194	514	Gene3D	G3DSA:3.40.50.620	HUPs
194	514	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
2	186	ProSiteProfiles	PS51278	Glutamine amidotransferase type 2 domain profile.
2	186	InterPro	IPR017932	Glutamine amidotransferase type 2 domain
213	456	CDD	cd01991	Asn_Synthase_B_C
213	456	InterPro	IPR001962	Asparagine synthase
2	193	Gene3D	G3DSA:3.60.20.10	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
2	193	InterPro	IPR029055	Nucleophile aminohydrolases, N-terminal
1	196	SUPERFAMILY	SSF56235	N-terminal nucleophile aminohydrolases (Ntn hydrolases)
1	196	InterPro	IPR029055	Nucleophile aminohydrolases, N-terminal
211	366	Pfam	PF00733	Asparagine synthase
211	366	InterPro	IPR001962	Asparagine synthase
2	193	FunFam	G3DSA:3.60.20.10:FF:000037	Asparagine synthetase B

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_A0A0H3GQ75	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_31943	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				0.995
28				0.271
2				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	Score	Probability
1	35.22	0.952
2	2.28	0.057
3	2.19	0.052
4	1.92	0.039
5	1.53	0.022

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				0.996

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	40.13	0.963
2	2.87	0.091
3	2.72	0.081
4	2.1	0.048
5	1.69	0.029

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.

62 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
APC	1JGT	P0DJQ7	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
CMA	1JGT	P0DJQ7	246.3 Da LogP -1.23 TPSA 148.5	1 viol.	✓ Clean	`C(C[C@@H](C(=O)O)NCCC(=O)O)CNC(=N)N`
IOT	1MBZ	P0DJQ7	561.4 Da LogP -3.01 TPSA 303.4	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
IUM	1CT9	P22106	270.0 Da LogP -2.38 TPSA 46.1	✓ Ro5	✓ Clean	`[O-][U+4][O-]`
ONL	6GQ3	P08243	145.2 Da LogP -0.23 TPSA 80.4	✓ Ro5	✓ Clean	`CC(=O)CC[C@@H](C(=O)O)N`
PCX	1MC1	P0DJQ7	228.3 Da LogP -1.06 TPSA 119.5	✓ Ro5	✓ Clean	`[H]/N=C(/N)\NCCC[C@@H](C(=O)O)N1CCC1=O`
POP	1MB9	P0DJQ7	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=O)(O)[O-]`
SSC	1Q19	Q9XB61	173.2 Da LogP -0.33 TPSA 86.6	✓ Ro5	✓ Clean	`C1C[C@H](N[C@@H]1CC(=O)O)C(=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
CHEMBL1627258	P08243	8.60	495.4 Da LogP -2.35 TPSA 264.6	2 viol.	✓ Clean	`C[S+]([O-])(C[C@H](N)C(=O)O)=NP(=O)(O)OC[C@H]1O…`
CHEMBL2153507	P08243	8.10	451.4 Da LogP -1.80 TPSA 227.3	1 viol.	✓ Clean	`C[S+]([O-])(CCN)=NP(=O)(O)OC[C@H]1O[C@@H](n2cnc…`
CHEMBL2153508	P08243	6.51	480.4 Da LogP -1.28 TPSA 238.6	1 viol.	✓ Clean	`C[S+]([O-])(CCC(=O)O)=NP(=O)(O)OC[C@H]1O[C@@H](…`
CHEMBL3250951	P49088	—	184.2 Da LogP -2.29 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CS(=O)(=O)NO)C(=O)O`

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
ZINC1530510	1.000	246.3 Da LogP -1.23 TPSA 148.5	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NCCC(=O)O)C(=O)O`
ZINC105469665	0.855	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614	0.855	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC219330894	0.855	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852	0.855	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853	0.855	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854	0.855	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855	0.855	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC12360002	0.821	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703	0.821	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599	0.821	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165	0.821	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053	0.821	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433	0.821	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898	0.821	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.821	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020	0.821	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.821	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022	0.821	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC13518964	0.815	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1571045	0.815	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.815	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931	0.815	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.815	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.815	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.815	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.815	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.815	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.815	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442	0.815	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167	0.815	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC4096224	0.768	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC105372833	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC1529261	0.722	304.3 Da LogP -1.39 TPSA 185.8	1 viol.	✓ Clean	`N=C(N)NCCC[C@@H](N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC1529262	0.722	304.3 Da LogP -1.39 TPSA 185.8	1 viol.	✓ Clean	`N=C(N)NCCC[C@@H](N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC1529939	0.722	304.3 Da LogP -1.39 TPSA 185.8	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC1529940	0.722	304.3 Da LogP -1.39 TPSA 185.8	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC5615251	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615253	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC5615258	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615263	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC12503850	0.705	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066	0.705	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786	0.705	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246	0.705	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC1582675	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486730	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`

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.