KpKP13 Protein target profile

Isoaspartyl peptidase

Accession: KP13_04286

Gene: iaaA AHE45519.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GLX8

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Length 313

Pocket druggability (P2Rank · AlphaFold DB model) 0.065

Direct ligand evidence 0 56 total records

Functional annotation 0 EC 1 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Human identity (%): 42.017 Lower values reduce human off-target concern.
Human E-value: 1.96e-22
Gut microbiome similarity: 1.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 92.85 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.065

Structure A0A0H3GLX8

Pocket Pocket 1

Druggability (FPocket) 0.344

Structure A0A0H3GLX8

Pocket Pocket 1

ColabFold model

P2Rank 0.306 · Pocket 1

FPocket 0.42 · Pocket 8

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 87 / 4744 genomes with a hit

Prevalence 1.8%

Sequence

Primary amino-acid sequence viewer.

MGKAVIAIHGGAGAISRAQMTPEREREYVAALSTIVESGQKMLAAGASALDAVTEAVRLLEECPLFNAGMGAVFTRDQTHELDACVMDGYSLQAGAVAGVKHLRNPVLAARLVLEKSPHVLLIGEGAENFAISHGMARVDNDLFSTPERLLQLQEAKAGGEIILDHHAAPLDERQKMGTVGAVALDLAGNLAAATSTGGMTNKLPGRVGDSPLPGAGCYANNASVAVSCTGTGEVFMRTLAAYDIAALMEYGQLSLYSACERVVMEKLPALGGSGGLIAVDREGNVVLPFNSEGMYRAWCYAGDTPTIGIYRE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 GO

Subcellular localization

Localization: Unknown

Gene Ontology (GO)

GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

9 records

Show feature table

Start	End	DB	Term	Name
4	298	PANTHER	PTHR10188	L-ASPARAGINASE
4	298	InterPro	IPR000246	Peptidase T2, asparaginase 2
179	313	FunFam	G3DSA:3.60.20.30:FF:000001	Isoaspartyl peptidase/L-asparaginase
5	310	Pfam	PF01112	Asparaginase
5	310	InterPro	IPR000246	Peptidase T2, asparaginase 2
4	310	SUPERFAMILY	SSF56235	N-terminal nucleophile aminohydrolases (Ntn hydrolases)
4	310	InterPro	IPR029055	Nucleophile aminohydrolases, N-terminal
5	299	CDD	cd04701	Asparaginase_2
179	313	Gene3D	G3DSA:3.60.20.30	(Glycosyl)asparaginase

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.065

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Surrounding area

Pocket 2 P2Rank #2

0.04

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Surrounding area

Pocket 3 P2Rank #3

0.005

Likely same site as FPocket 1 6.5 Å 7 shared residues 100% of smaller site

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #1

0.344 Unusual size

Likely same site as P2Rank 3 6.5 Å 7 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:179-179 Nucleophile

UniProt: Binding site:207-210

UniProt: Binding site:230-233

UniProt: Site:178-179 Cleavage; by autolysis

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.306

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Surrounding area

Pocket 2 P2Rank #2

0.156

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Surrounding area

Pocket 3 P2Rank #3

0.017

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #8

0.42

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Surrounding area

Pocket 2 FPocket #10

0.4

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Surrounding area

Pocket 3 FPocket #15

0.279

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Surrounding area

Pocket 4 FPocket #3

0.235

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3GLX8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04286	ColabFold	—	—	full sequence	—	Loaded

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

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 10 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 5 direct and transferred ChEMBL records

Proposed compounds 46 similarity-based ZINC candidates

Best available ligand signal

DTT PDB via homolog 154.3 Da · LogP -0.43 · TPSA 40.5 Open detail RCSB PDB

FLC PDB via homolog Detail RCSB PDB

MLI PDB via homolog Detail RCSB PDB

SD4 PDB via homolog Detail RCSB PDB

TAM PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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
DTT RCSB PDB	4ZM9	Q7L266	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
FLC RCSB PDB	4ZM9	Q7L266	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
MLI RCSB PDB	4PVP	Q7L266	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
SD4 RCSB PDB	4R4Y	Q47898	148.1 Da LogP -1.71 TPSA 112.6	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)N)C(=O)NO`
TAM RCSB PDB	3TKJ	Q7L266	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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL1091971 ChEMBL	Q9H6P5	—	416.1 Da LogP -1.60 TPSA 115.1	✓ Ro5	✓ Clean	`O=[As](O)(O)c1ccc(Cc2ccc([As](=O)(O)O)cc2)cc1`
CHEMBL570439 ChEMBL	Q9H6P5	—	656.7 Da LogP -2.39 TPSA 275.7	2 viol.	✓ Clean	`CC[C@H](C)[C@H](NC(C)=O)C(=O)N[C@@H](CO)C(=O)N[…`
CHEMBL570714 ChEMBL	Q9H6P5	—	676.8 Da LogP -2.19 TPSA 280.3	2 viol.	✓ Clean	`CC[C@H](C)[C@H](NC(C)=O)C(=O)N[C@@H](CO)C(=O)N[…`
CHEMBL570859 ChEMBL	Q9H6P5	—	640.7 Da LogP -1.60 TPSA 263.2	2 viol.	✓ Clean	`CC[C@H](C)[C@H](NC(C)=O)C(=O)N[C@@H](CO)C(=O)N[…`
CHEMBL576100 ChEMBL	Q9H6P5	—	676.8 Da LogP -2.19 TPSA 280.3	2 viol.	✓ Clean	`CC[C@H](C)[C@H](NC(C)=O)C(=O)N[C@@H](CO)C(=O)N[…`

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
ZINC2575038 ZINC	0.625	205.3 Da LogP 0.00 TPSA 86.7	✓ Ro5	✓ Clean	`NC(CCCO)(CCCO)CCCO`
ZINC1709621 ZINC	0.600	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)N[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC1709623 ZINC	0.600	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)N[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC1709624 ZINC	0.600	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CC(=O)N[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC1709622 ZINC	0.571	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CC(=O)N[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC1575288 ZINC	0.560	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O`
ZINC1575289 ZINC	0.560	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O`
ZINC1575290 ZINC	0.560	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)O`
ZINC1575291 ZINC	0.560	248.2 Da LogP -2.17 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)O`
ZINC5131760 ZINC	0.560	237.2 Da LogP -0.94 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@@H](CS[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC5131761 ZINC	0.560	237.2 Da LogP -0.94 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@H](CS[C@@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC5131922 ZINC	0.560	237.2 Da LogP -0.94 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@@H](CS[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC5131923 ZINC	0.560	237.2 Da LogP -0.94 TPSA 137.9	✓ Ro5	✓ Clean	`N[C@H](CS[C@H](CC(=O)O)C(=O)O)C(=O)O`
ZINC2123927 ZINC	0.538	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@@H](N)CC(=O)O)C(=O)O`
ZINC2560978 ZINC	0.538	204.2 Da LogP -1.62 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)C[C@H](N)C(=O)O)C(=O)O`
ZINC1730666 ZINC	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CSC[C@H](N)C(=O)O)C(=O)O`
ZINC1730667 ZINC	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CSC[C@H](N)C(=O)O)C(=O)O`
ZINC1730669 ZINC	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CSC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055005 ZINC	0.524	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O`
ZINC3055007 ZINC	0.524	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055010 ZINC	0.524	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC100655912 ZINC	0.519	478.4 Da LogP -4.25 TPSA 299.8	1 viol.	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)N[C@H](…`
ZINC100655916 ZINC	0.519	478.4 Da LogP -4.25 TPSA 299.8	1 viol.	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)N[C@@H]…`
ZINC255993703 ZINC	0.519	478.4 Da LogP -4.25 TPSA 299.8	1 viol.	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)N[C@H](…`
ZINC4533843 ZINC	0.519	363.3 Da LogP -3.21 TPSA 233.4	1 viol.	✓ Clean	`N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@…`
ZINC4533848 ZINC	0.519	478.4 Da LogP -4.25 TPSA 299.8	1 viol.	✓ Clean	`N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@…`
ZINC4533853 ZINC	0.519	478.4 Da LogP -4.25 TPSA 299.8	1 viol.	✓ Clean	`N[C@H](CC(=O)O)C(=O)N[C@H](CC(=O)O)C(=O)N[C@@H]…`
ZINC1555366 ZINC	0.500	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1555367 ZINC	0.500	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1555369 ZINC	0.500	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1577651 ZINC	0.500	234.2 Da LogP -0.66 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C[C@H](C(=O)O)[C@@H](CC(=O)O)C(=O)O`
ZINC1577652 ZINC	0.500	234.2 Da LogP -0.66 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C[C@@H](C(=O)O)[C@@H](CC(=O)O)C(=O)O`
ZINC1577653 ZINC	0.500	234.2 Da LogP -0.66 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C[C@H](C(=O)O)[C@H](CC(=O)O)C(=O)O`
ZINC1720127 ZINC	0.500	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1720128 ZINC	0.500	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720130 ZINC	0.500	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC22923898 ZINC	0.500	307.3 Da LogP -3.04 TPSA 199.3	1 viol.	✓ Clean	`N[C@@H](CN[C@@H](CN[C@@H](CC(=O)O)C(=O)O)C(=O)O…`
ZINC22923905 ZINC	0.500	307.3 Da LogP -3.04 TPSA 199.3	1 viol.	✓ Clean	`N[C@@H](CN[C@H](CN[C@@H](CC(=O)O)C(=O)O)C(=O)O)…`
ZINC22930737 ZINC	0.500	307.3 Da LogP -3.04 TPSA 199.3	1 viol.	✓ Clean	`N[C@H](CN[C@H](CN[C@@H](CC(=O)O)C(=O)O)C(=O)O)C…`
ZINC23355305 ZINC	0.500	307.3 Da LogP -3.04 TPSA 199.3	1 viol.	✓ Clean	`N[C@H](CN[C@@H](CN[C@@H](CC(=O)O)C(=O)O)C(=O)O)…`
ZINC2384839 ZINC	0.500	232.2 Da LogP -0.99 TPSA 129.7	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)[C@@H](N)CC(=O)O)C(=O)O`
ZINC2560328 ZINC	0.500	239.1 Da LogP 1.53 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](CC(C(F)(F)F)C(F)(F)F)C(=O)O`
ZINC3623257 ZINC	0.500	202.2 Da LogP -0.85 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](C/C=C/C[C@@H](N)C(=O)O)C(=O)O`
ZINC4348166 ZINC	0.500	239.1 Da LogP 1.53 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](CC(C(F)(F)F)C(F)(F)F)C(=O)O`
ZINC4580672 ZINC	0.500	202.2 Da LogP -0.85 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](C/C=C/C[C@H](N)C(=O)O)C(=O)O`
ZINC4580676 ZINC	0.500	202.2 Da LogP -0.85 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](C/C=C/C[C@@H](N)C(=O)O)C(=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.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GLX8

Chemistry

ChEMBL CHEMBL1091971 ChEMBL CHEMBL570439 ChEMBL CHEMBL570714 ChEMBL CHEMBL570859 ChEMBL CHEMBL576100

Isoaspartyl peptidase

Target candidate with partial support; inspect missing evidence before prioritizing.

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Sequence

Functional annotations

Subcellular localization

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry