Amino acids
362
Annotations
8
Features
40
PDB binders
9
Druggability
0.824
Overview
Basic information about this protein and its source genome.
- Accession
- PA1337
- Gene
- ansB PA1337
- Status
- annotated
- Amino acids
- 362
- Structure source
- AlphaFold
EC
GO
GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
GO:0004067 Catalysis of the reaction: L-asparagine + H2O = L-aspartate + NH4+.
GO:0050417 Catalysis of the reactions: H2O + L-glutamine = NH4 + L-glutamate; and H2O + L-asparagine = NH4 + L-aspartate.
GO:0004359 Catalysis of the reaction: L-glutamine + H2O = L-glutamate + NH4+.
GO:0006530 The chemical reactions and pathways resulting in the breakdown of L-asparagine.
GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- Localization
- Periplasmic
Selected Druggability evidence
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
0.824
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)
1Gene Ontology (GO)
7- GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
- GO:0004067 Catalysis of the reaction: L-asparagine + H2O = L-aspartate + NH4+.
- GO:0050417 Catalysis of the reactions: H2O + L-glutamine = NH4 + L-glutamate; and H2O + L-asparagine = NH4 + L-aspartate.
- GO:0004359 Catalysis of the reaction: L-glutamine + H2O = L-glutamate + NH4+.
- GO:0006530 The chemical reactions and pathways resulting in the breakdown of L-asparagine.
- GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
- GO:0006528 The chemical reactions and pathways involving asparagine, 2-amino-3-carbamoylpropanoic acid.
Sequence Features
Domain/signature hits from InterPro and related databases.
40 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 34 | 361 | SUPERFAMILY | SSF53774 | Glutaminase/Asparaginase |
| 34 | 361 | InterPro | IPR036152 | Asparaginase/glutaminase-like superfamily |
| 32 | 247 | FunFam | G3DSA:3.40.50.1170:FF:000001 | L-asparaginase 2 |
| 25 | 362 | NCBIfam | TIGR00520 | type II asparaginase |
| 25 | 362 | InterPro | IPR004550 | L-asparaginase, type II |
| 1 | 3 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 118 | 128 | ProSitePatterns | PS00917 | Asparaginase / glutaminase active site signature 2. |
| 118 | 128 | InterPro | IPR027475 | Asparaginase/glutaminase, active site 2 |
| 249 | 359 | Pfam | PF17763 | Glutaminase/Asparaginase C-terminal domain |
| 249 | 359 | InterPro | IPR040919 | Asparaginase/glutaminase, C-terminal |
| 249 | 361 | Gene3D | G3DSA:3.40.50.40 | - |
| 249 | 361 | InterPro | IPR027473 | L-asparaginase, C-terminal |
| 117 | 135 | PRINTS | PR00139 | Asparaginase/glutaminase family signature |
| 117 | 135 | InterPro | IPR006034 | Asparaginase/glutaminase-like |
| 295 | 313 | PRINTS | PR00139 | Asparaginase/glutaminase family signature |
| 295 | 313 | InterPro | IPR006034 | Asparaginase/glutaminase-like |
| 37 | 48 | PRINTS | PR00139 | Asparaginase/glutaminase family signature |
| 37 | 48 | InterPro | IPR006034 | Asparaginase/glutaminase-like |
| 39 | 47 | ProSitePatterns | PS00144 | Asparaginase / glutaminase active site signature 1. |
| 39 | 47 | InterPro | IPR020827 | Asparaginase/glutaminase, active site 1 |
| 36 | 226 | Pfam | PF00710 | Asparaginase, N-terminal |
| 36 | 226 | InterPro | IPR027474 | L-asparaginase, N-terminal |
| 1 | 25 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 59 | 356 | CDD | cd00411 | L-asparaginase_like |
| 4 | 19 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 35 | 362 | ProSiteProfiles | PS51732 | Asparaginase / glutaminase domain profile. |
| 35 | 362 | InterPro | IPR006034 | Asparaginase/glutaminase-like |
| 31 | 362 | PIRSF | PIRSF001220 | L-ASNase_gatD |
| 31 | 362 | InterPro | IPR006034 | Asparaginase/glutaminase-like |
| 35 | 247 | Gene3D | G3DSA:3.40.50.1170 | - |
| 35 | 247 | InterPro | IPR037152 | L-asparaginase, N-terminal domain superfamily |
| 1 | 25 | SignalP_EUK | SignalP-noTM | SignalP-noTM |
| 20 | 25 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 36 | 356 | SMART | SM00870 | Asparaginase_2 |
| 36 | 356 | InterPro | IPR006034 | Asparaginase/glutaminase-like |
| 33 | 362 | PIRSF | PIRSF500176 | L_ASNase |
| 26 | 362 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 1 | 25 | SignalP_GRAM_POSITIVE | SignalP-TM | SignalP-TM |
| 31 | 358 | PANTHER | PTHR11707 | L-ASPARAGINASE |
| 31 | 358 | InterPro | IPR006034 | Asparaginase/glutaminase-like |
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 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA1337
|
AlphaFold | — | — | full sequence | — | Viewing |
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 |
|---|---|---|---|---|---|---|---|
| 6 | 0.824 | ||||||
| 3 | 0.602 | ||||||
| 2 | 0.342 |
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 |
|---|---|---|---|---|---|---|
| AEI | P00805 | 234.2 Da LogP -1.87 TPSA 152.9 | ✓ Ro5 | ✓ Clean |
C[C@H]([C@@H](C(=O)O)N)OC(=O)C[C@@H](C(=O)O)N
|
|
| CAB | P10182 | 163.1 Da LogP -2.33 TPSA 120.8 | ✓ Ro5 | ✓ Clean |
C([C@@H](C(=O)O)N)C(C=O)(O)O
|
|
| DAS | P06608 | 133.1 Da LogP -1.13 TPSA 100.6 | ✓ Ro5 | ✓ Clean |
C([C@H](C(=O)O)N)C(=O)O
|
|
| DDO | P06608 | 147.2 Da LogP -0.44 TPSA 83.5 | ✓ Ro5 | ✓ Clean |
C(CCO)C[C@H](C(=O)O)N
|
|
| DO2 | P10182 | 177.2 Da LogP -1.94 TPSA 120.8 | ✓ Ro5 | ✓ Clean |
C(CC(C=O)(O)O)[C@@H](C(=O)O)N
|
|
| FLC | P00805 | 189.1 Da LogP -5.25 TPSA 140.6 | ✓ Ro5 | ✓ Clean |
C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
|
|
| LDO | P06608 | 147.2 Da LogP -0.44 TPSA 83.5 | ✓ Ro5 | ✓ Clean |
C(CCO)C[C@@H](C(=O)O)N
|
|
| NH4 | P10182 | 18.0 Da LogP 0.38 TPSA 36.5 | ✓ Ro5 | ✓ Clean |
[NH4+]
|
|
| SIN | P06608 | 118.1 Da LogP -0.06 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C(CC(=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).
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 |
|---|---|---|---|---|---|
| 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
|
| 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
|
| 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(=…
|
| ZINC1709621 | 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 | 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 | 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 | 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
|
| ZINC4023216 | 0.583 | 274.4 Da LogP 2.67 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
O=C(O)C(CCCCCCCCCCCO)C(=O)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
|
| ZINC1572706 | 0.563 | 260.2 Da LogP -1.05 TPSA 132.8 | ✓ Ro5 | ✓ Clean |
O=C(O)CCC(=O)NCCNC(=O)CCC(=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
|
| ZINC1575288 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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
|
| ZINC1850353 | 0.556 | 206.1 Da LogP -0.86 TPSA 132.1 | ✓ Ro5 | ✓ Clean |
O=C(O)CC(O)(CC(=O)O)CC(=O)O
|
| ZINC2123927 | 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 | 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
|
| ZINC35465466 | 0.529 | 244.3 Da LogP 2.24 TPSA 91.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCC(=O)CCC(=O)O
|
| ZINC39208104 | 0.529 | 262.2 Da LogP -0.20 TPSA 127.2 | ✓ Ro5 | ✓ Clean |
O=C(O)CCC(=O)OCCOC(=O)CCC(=O)O
|
| ZINC1730666 | 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 | 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 | 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 | 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 | 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 | 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
|
| ZINC13398014 | 0.522 | 220.2 Da LogP -1.07 TPSA 110.1 | ✓ Ro5 | ✓ Clean |
COC(=O)CC(O)(CC(=O)OC)C(=O)O
|
| ZINC3861629 | 0.522 | 206.1 Da LogP -1.16 TPSA 121.1 | ✓ Ro5 | ✓ Clean |
COC(=O)C(O)(CC(=O)O)CC(=O)O
|
| ZINC100655912 | 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 | 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 | 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 | 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 | 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 | 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]…
|
| ZINC100969993 | 0.500 | 359.5 Da LogP 2.70 TPSA 123.9 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCNC(=O)C[C@](O)(CC(=O)O)C(=O)O
|
| ZINC100969996 | 0.500 | 359.5 Da LogP 2.70 TPSA 123.9 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCNC(=O)C[C@@](O)(CC(=O)O)C(=O)O
|
| ZINC1555369 | 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
|
| ZINC1711854 | 0.500 | 248.2 Da LogP -0.13 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
O=C(O)CC(CC(=O)O)(CC(=O)O)CC(=O)O
|
| ZINC38682833 | 0.500 | 286.3 Da LogP -0.61 TPSA 115.2 | ✓ Ro5 | ✓ Clean |
O=C(O)CCC(=O)N1CCN(C(=O)CCC(=O)O)CC1
|
| ZINC4348166 | 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
|
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.