Amino acids
373
Annotations
8
Features
27
PDB binders
11
Druggability
0.61
Overview
Basic information about this protein and its source genome.
- Accession
- PA2509
- Gene
- catB PA2509
- Status
- annotated
- Amino acids
- 373
- Structure source
- AlphaFold
GO
GO:0018850 Catalysis of the reaction: 2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3-chloro-cis,cis-muconate.
GO:0016836 Catalysis of the cleavage of a carbon-oxygen bond by elimination of water.
GO:0030145 Binding to a manganese ion (Mn).
GO:0018849 Catalysis of the reaction: 2,5-dihydro-5-oxofuran-2-acetate = cis,cis-hexadienedioate.
GO:0016854 Catalysis of a reaction that alters the configuration of one or more chiral centers in a molecule.
GO:0009063 The chemical reactions and pathways resulting in the breakdown of amino acids, organic acids containing one or more amino substituents.
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- Localization
- Cytoplasmic
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
0.61
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
8 GO
Gene Ontology (GO)
8- GO:0018850 Catalysis of the reaction: 2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3-chloro-cis,cis-muconate.
- GO:0016836 Catalysis of the cleavage of a carbon-oxygen bond by elimination of water.
- GO:0030145 Binding to a manganese ion (Mn).
- GO:0018849 Catalysis of the reaction: 2,5-dihydro-5-oxofuran-2-acetate = cis,cis-hexadienedioate.
- GO:0016854 Catalysis of a reaction that alters the configuration of one or more chiral centers in a molecule.
- GO:0009063 The chemical reactions and pathways resulting in the breakdown of amino acids, organic acids containing one or more amino substituents.
- GO:0009234 The chemical reactions and pathways resulting in the formation of any of the menaquinones. Structurally, menaquinones consist of a methylated naphthoquinone ring structure and side chains composed of a variable number of unsaturated isoprenoid residues. Menaquinones that have vitamin K activity and are known as vitamin K2.
- GO:0006518 The chemical reactions and pathways involving peptides, compounds of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
Sequence Features
Domain/signature hits from InterPro and related databases.
27 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 122 | 357 | Gene3D | G3DSA:3.20.20.120 | - |
| 122 | 357 | InterPro | IPR036849 | Enolase-like, C-terminal domain superfamily |
| 152 | 365 | Pfam | PF13378 | Enolase C-terminal domain-like |
| 152 | 365 | InterPro | IPR029065 | Enolase C-terminal domain-like |
| 2 | 373 | SFLD | SFLDG01258 | (chloro)muconate cycloisomerase (syn) like |
| 2 | 373 | InterPro | IPR013370 | Muconate/chloromuconate cycloisomerase |
| 32 | 369 | Gene3D | G3DSA:3.30.390.10 | - |
| 32 | 369 | InterPro | IPR029017 | Enolase-like, N-terminal |
| 147 | 245 | SMART | SM00922 | MR_MLE_2 |
| 147 | 245 | InterPro | IPR013342 | Mandelate racemase/muconate lactonizing enzyme, C-terminal |
| 6 | 372 | NCBIfam | TIGR02534 | muconate/chloromuconate family cycloisomerase |
| 6 | 372 | InterPro | IPR013370 | Muconate/chloromuconate cycloisomerase |
| 360 | 373 | Coils | Coil | Coil |
| 6 | 369 | CDD | cd03318 | MLE |
| 6 | 369 | InterPro | IPR013370 | Muconate/chloromuconate cycloisomerase |
| 13 | 129 | Pfam | PF02746 | Mandelate racemase / muconate lactonizing enzyme, N-terminal domain |
| 13 | 129 | InterPro | IPR013341 | Mandelate racemase/muconate lactonizing enzyme, N-terminal domain |
| 5 | 368 | PANTHER | PTHR48073 | O-SUCCINYLBENZOATE SYNTHASE-RELATED |
| 195 | 226 | ProSitePatterns | PS00909 | Mandelate racemase / muconate lactonizing enzyme family signature 2. |
| 195 | 226 | InterPro | IPR018110 | Mandelate racemase/muconate lactonizing enzyme, conserved site |
| 2 | 373 | SFLD | SFLDS00001 | Enolase |
| 129 | 370 | SUPERFAMILY | SSF51604 | Enolase C-terminal domain-like |
| 129 | 370 | InterPro | IPR036849 | Enolase-like, C-terminal domain superfamily |
| 6 | 130 | SUPERFAMILY | SSF54826 | Enolase N-terminal domain-like |
| 6 | 130 | InterPro | IPR029017 | Enolase-like, N-terminal |
| 104 | 129 | ProSitePatterns | PS00908 | Mandelate racemase / muconate lactonizing enzyme family signature 1. |
| 104 | 129 | InterPro | IPR018110 | Mandelate racemase/muconate lactonizing enzyme, conserved site |
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
PA2509
|
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 |
|---|---|---|---|---|---|---|---|
| 2 | 0.422 | ||||||
| 1 | 0.265 |
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.
61 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 |
|---|---|---|---|---|---|---|
| 5CR | Q44244 | 207.2 Da LogP 0.82 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccccc1)C(=O)O
|
|
| AME | Q44244 | 191.3 Da LogP 0.33 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](CCSC)C(=O)O
|
|
| GAE | Q8EMJ9 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
[C@H]([C@H]([C@@H](C(=O)O)O)O)([C@H](C(=O)O)O)O
|
|
| LMR | Q8EMJ9 | 134.1 Da LogP -1.09 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
C([C@@H](C(=O)O)O)C(=O)O
|
|
| MUC | A0QTN8 | 142.1 Da LogP -0.06 TPSA 63.6 | ✓ Ro5 | ✓ Clean |
C1=CC(=O)O[C@H]1CC(=O)O
|
|
| NPG | Q44244 | 251.2 Da LogP 0.79 TPSA 103.7 | ✓ Ro5 | ✓ Clean |
c1ccc(cc1)[C@H](C(=O)O)NC(=O)CCC(=O)O
|
|
| NPQ | Q44244 | 257.3 Da LogP 1.97 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccc2ccccc2c1)C(=O)O
|
|
| NSK | Q81IL5 | 246.3 Da LogP -0.45 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
C(CCN)C[C@@H](C(=O)O)NC(=O)CCC(=O)O
|
|
| OSB | Q44244 | 222.2 Da LogP 1.43 TPSA 91.7 | ✓ Ro5 | ✓ Clean |
c1ccc(c(c1)C(=O)CCC(=O)O)C(=O)O
|
|
| SMG | Q44244 | 249.3 Da LogP 0.17 TPSA 103.7 | ✓ Ro5 | ✓ Clean |
CSCC[C@H](C(=O)O)NC(=O)CCC(=O)O
|
|
| SUG | Q81IL5 | 274.3 Da LogP -1.32 TPSA 165.6 | 1 viol. | ✓ Clean |
C(C[C@@H](C(=O)O)NC(=O)CCC(=O)O)CNC(=N)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).
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 |
|---|---|---|---|---|---|
| ZINC1081446 | 1.000 | 257.3 Da LogP 1.97 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H](Cc1ccc2ccccc2c1)C(=O)O
|
| ZINC12359024 | 1.000 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O
|
| ZINC128209 | 1.000 | 257.3 Da LogP 1.97 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccc2ccccc2c1)C(=O)O
|
| ZINC13533920 | 1.000 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC135391 | 1.000 | 207.2 Da LogP 0.82 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccccc1)C(=O)O
|
| ZINC135392 | 1.000 | 207.2 Da LogP 0.82 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H](Cc1ccccc1)C(=O)O
|
| ZINC1529628 | 1.000 | 274.3 Da LogP -1.32 TPSA 165.6 | 1 viol. | ✓ Clean |
N=C(N)NCCC[C@H](NC(=O)CCC(=O)O)C(=O)O
|
| ZINC1532740 | 1.000 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O
|
| ZINC1549593 | 1.000 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC2013424 | 1.000 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O
|
| ZINC3581021 | 1.000 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC3860635 | 1.000 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O
|
| ZINC5783661 | 1.000 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O
|
| ZINC6072527 | 1.000 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC1576657 | 0.871 | 354.4 Da LogP 1.55 TPSA 95.5 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccccc1)…
|
| ZINC1604722 | 0.870 | 326.3 Da LogP 2.93 TPSA 108.7 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccccc1C(=O)CCC(=O)c1ccccc1C(=O)O
|
| ZINC1866114950 | 0.844 | 260.3 Da LogP -0.06 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
NCCCC[C@H](NC(=O)CCCC(=O)O)C(=O)O
|
| ZINC59901848 | 0.839 | 283.3 Da LogP 2.49 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O
|
| ZINC59950807 | 0.839 | 283.3 Da LogP 2.49 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O
|
| ZINC2383349774 | 0.838 | 330.4 Da LogP 0.24 TPSA 165.6 | 1 viol. | ✓ Clean |
N=C(N)NCCC[C@H](NC(=O)CCCCCCC(=O)O)C(=O)O
|
| ZINC1530138 | 0.806 | 217.3 Da LogP -0.97 TPSA 118.4 | ✓ Ro5 | ✓ Clean |
NCCCC[C@H](NC(=O)CCN)C(=O)O
|
| ZINC3069075 | 0.800 | 205.3 Da LogP 1.32 TPSA 46.2 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H](Cc1ccccc1)C(C)=O
|
| ZINC333188 | 0.800 | 205.3 Da LogP 1.32 TPSA 46.2 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccccc1)C(C)=O
|
| ZINC2567641 | 0.765 | 311.3 Da LogP 2.05 TPSA 83.5 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O
|
| ZINC34254310 | 0.765 | 311.3 Da LogP 2.05 TPSA 83.5 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O
|
| ZINC59991742 | 0.763 | 333.4 Da LogP 3.19 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=C(Cc1ccc2ccccc2c1)N[C@@H](Cc1ccccc1)C(=O)O
|
| ZINC156395 | 0.750 | 223.2 Da LogP 0.52 TPSA 86.6 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)O
|
| ZINC1570988 | 0.750 | 221.3 Da LogP 1.13 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccc(C)cc1)C(=O)O
|
| ZINC2504804 | 0.750 | 370.4 Da LogP 1.25 TPSA 115.7 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccc(O)cc…
|
| ZINC2508275 | 0.750 | 370.4 Da LogP 1.25 TPSA 115.7 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1cccc…
|
| ZINC2983276 | 0.750 | 370.4 Da LogP 1.25 TPSA 115.7 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@H](Cc1ccc(O)cc…
|
| ZINC2983277 | 0.750 | 370.4 Da LogP 1.25 TPSA 115.7 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H](Cc1ccccc1)C(=O)N[C@H](Cc1ccc(O)cc1…
|
| ZINC396118 | 0.750 | 223.2 Da LogP 0.52 TPSA 86.6 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H](Cc1ccc(O)cc1)C(=O)O
|
| ZINC399346 | 0.750 | 206.2 Da LogP 0.22 TPSA 72.2 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccccc1)C(N)=O
|
| ZINC399347 | 0.750 | 206.2 Da LogP 0.22 TPSA 72.2 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H](Cc1ccccc1)C(N)=O
|
| ZINC4117655 | 0.750 | 370.4 Da LogP 1.25 TPSA 115.7 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccc(O)c…
|
| ZINC6845290 | 0.750 | 221.3 Da LogP 1.13 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H](Cc1ccc(C)cc1)C(=O)O
|
| ZINC50916638 | 0.742 | 237.2 Da LogP 0.40 TPSA 103.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CC(=O)N[C@H](C(=O)O)c1ccccc1
|
| ZINC50916640 | 0.742 | 237.2 Da LogP 0.40 TPSA 103.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CC(=O)N[C@@H](C(=O)O)c1ccccc1
|
| ZINC4760151 | 0.735 | 264.3 Da LogP -0.07 TPSA 95.5 | ✓ Ro5 | ✓ Clean |
CC(=O)NCC(=O)N[C@@H](Cc1ccccc1)C(=O)O
|
| ZINC4760152 | 0.735 | 264.3 Da LogP -0.07 TPSA 95.5 | ✓ Ro5 | ✓ Clean |
CC(=O)NCC(=O)N[C@H](Cc1ccccc1)C(=O)O
|
| ZINC399541 | 0.730 | 313.4 Da LogP 2.40 TPSA 75.6 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccc(OCc2ccccc2)cc1)C(=O)O
|
| ZINC399542 | 0.730 | 313.4 Da LogP 2.40 TPSA 75.6 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H](Cc1ccc(OCc2ccccc2)cc1)C(=O)O
|
| ZINC128390 | 0.727 | 286.1 Da LogP 1.58 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccc(Br)cc1)C(=O)O
|
| ZINC154536 | 0.727 | 225.2 Da LogP 0.96 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccc(F)cc1)C(=O)O
|
| ZINC2510605 | 0.727 | 222.2 Da LogP 0.40 TPSA 92.4 | ✓ Ro5 | Alert |
CC(=O)N[C@@H](Cc1ccc(N)cc1)C(=O)O
|
| ZINC2560837 | 0.727 | 286.1 Da LogP 1.58 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H](Cc1ccc(Br)cc1)C(=O)O
|
| ZINC2560838 | 0.727 | 220.3 Da LogP 0.48 TPSA 58.2 | ✓ Ro5 | ✓ Clean |
CNC(=O)[C@H](Cc1ccccc1)NC(C)=O
|
| ZINC399446 | 0.727 | 241.7 Da LogP 1.47 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@@H](Cc1ccc(Cl)cc1)C(=O)O
|
| ZINC399561 | 0.727 | 333.1 Da LogP 1.42 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(=O)N[C@H](Cc1ccc(I)cc1)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.