Overview
Basic information about this protein and its source genome.
- Accession
- PA0608
- Gene
- gph1 PA0608
- Status
- annotated
- Amino acids
- 272
- Structure source
- AlphaFold
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.
Sequence
Primary amino-acid sequence viewer.
MSAAEPFFATRLPRLVMFDLDGTLVDSVPDLTAAVDSMLASFGRPPAGIEKVRQWIGNGARVLVRRALAGSIEHDGIGEEETEAALALFMEAYADSHALTEVYPGVVDTLKWLKRNGVEMALITNKPERFVAPLLDEMKLGRYFRWIIGGDTLPQQKPDPAALLFVMKMAGIEPEDALFVGDSRNDVLAAKAAGVRCAALTYGYNHGRPIAEEAPTLVIDNLRDLLPCADQAAEIVLPDDSLSPSDQRDQAVAVSKLWMKVIKALARWRWRA
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
6- GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
- GO:0046872 Binding to a metal ion.
- GO:0008967 Catalysis of the reaction: 2-phosphoglycolate + H2O = glycolate + phosphate.
- 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:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
- GO:0046295 The chemical reactions and pathways resulting in the formation of glycolate, the anion of hydroxyethanoic acid (glycolic acid).
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 14 | 227 | SFLD | SFLDG01135 | C1.5.6: HAD, Beta-PGM, Phosphatase Like |
| 13 | 230 | Hamap | MF_00495 | Phosphoglycolate phosphatase [gph]. |
| 13 | 230 | InterPro | IPR037512 | Phosphoglycolate phosphatase, prokaryotic |
| 94 | 220 | FunFam | G3DSA:3.40.50.1000:FF:000022 | Phosphoglycolate phosphatase |
| 13 | 226 | SUPERFAMILY | SSF56784 | HAD-like |
| 13 | 226 | InterPro | IPR036412 | HAD-like superfamily |
| 16 | 220 | Gene3D | G3DSA:3.40.50.1000 | - |
| 16 | 220 | InterPro | IPR023214 | HAD superfamily |
| 114 | 194 | NCBIfam | TIGR01549 | HAD-IA family hydrolase |
| 114 | 194 | InterPro | IPR006439 | HAD hydrolase, subfamily IA |
| 113 | 126 | PRINTS | PR00413 | Haloacid dehalogenase/epoxide hydrolase family signature |
| 113 | 126 | InterPro | IPR006439 | HAD hydrolase, subfamily IA |
| 13 | 24 | PRINTS | PR00413 | Haloacid dehalogenase/epoxide hydrolase family signature |
| 13 | 24 | InterPro | IPR006439 | HAD hydrolase, subfamily IA |
| 144 | 160 | PRINTS | PR00413 | Haloacid dehalogenase/epoxide hydrolase family signature |
| 144 | 160 | InterPro | IPR006439 | HAD hydrolase, subfamily IA |
| 162 | 182 | PRINTS | PR00413 | Haloacid dehalogenase/epoxide hydrolase family signature |
| 162 | 182 | InterPro | IPR006439 | HAD hydrolase, subfamily IA |
| 16 | 227 | NCBIfam | TIGR01449 | phosphoglycolate phosphatase |
| 16 | 227 | InterPro | IPR037512 | Phosphoglycolate phosphatase, prokaryotic |
| 15 | 226 | CDD | cd16417 | HAD_PGPase |
| 28 | 99 | Gene3D | G3DSA:1.10.150.240 | Putative phosphatase; domain 2 |
| 28 | 99 | InterPro | IPR023198 | Phosphoglycolate phosphatase-like, domain 2 |
| 14 | 227 | SFLD | SFLDS00003 | Haloacid Dehalogenase |
| 92 | 197 | NCBIfam | TIGR01509 | HAD-IA family hydrolase |
| 92 | 197 | InterPro | IPR006439 | HAD hydrolase, subfamily IA |
| 16 | 199 | Pfam | PF13419 | Haloacid dehalogenase-like hydrolase |
| 16 | 199 | InterPro | IPR041492 | Haloacid dehalogenase-like hydrolase |
| 3 | 227 | PANTHER | PTHR43434 | PHOSPHOGLYCOLATE PHOSPHATASE |
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...
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
PA0608
|
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 |
|---|---|---|---|---|---|---|---|
| 3 | 0.686 | ||||||
| 2 | 0.378 |
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.
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 |
|---|---|---|---|---|---|---|
| BO3 | B6SEG4 | 61.8 Da LogP -2.05 TPSA 60.7 | ✓ Ro5 | ✓ Clean |
B(O)(O)O
|
|
| NHE | B6YTD6 | 207.3 Da LogP 0.80 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
C1CCC(CC1)NCCS(=O)(=O)O
|
|
| PGA | P77247 | 156.0 Da LogP -0.82 TPSA 104.1 | ✓ Ro5 | ✓ Clean |
C(C(=O)O)OP(=O)(O)O
|
|
| TBU | B6YTD6 | 74.1 Da LogP 0.78 TPSA 20.2 | ✓ Ro5 | ✓ Clean |
CC(C)(C)O
|
|
| XBP | P95649 | 310.1 Da LogP -2.50 TPSA 191.0 | 1 viol. | ✓ Clean |
C([C@H]([C@@H](C(=O)COP(=O)(O)O)O)O)OP(=O)(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 |
|---|---|---|---|---|---|
| ZINC1710230 | 1.000 | 207.3 Da LogP 0.80 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCNC1CCCCC1
|
| ZINC2004372 | 0.786 | 221.3 Da LogP 1.19 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCCNC1CCCCC1
|
| ZINC38364153 | 0.786 | 235.3 Da LogP 1.58 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCCCNC1CCCCC1
|
| ZINC31259596 | 0.724 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(COP(=O)(O)O)[C@@H](O)[C@H](O)CO
|
| ZINC31259600 | 0.724 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(COP(=O)(O)O)[C@@H](O)[C@@H](O)CO
|
| ZINC3869804 | 0.724 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(COP(=O)(O)O)[C@H](O)[C@@H](O)CO
|
| ZINC3869805 | 0.724 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(COP(=O)(O)O)[C@H](O)[C@H](O)CO
|
| 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(=…
|
| 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
|
| 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
|
| ZINC19367005 | 0.560 | 224.4 Da LogP 2.83 TPSA 24.1 | ✓ Ro5 | ✓ Clean |
C1CCC(NCCNC2CCCCC2)CC1
|
| ZINC26468763 | 0.559 | 243.3 Da LogP -1.35 TPSA 100.5 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCN[C@@H]1CCS(=O)(=O)C1
|
| ZINC26468770 | 0.559 | 243.3 Da LogP -1.35 TPSA 100.5 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCN[C@H]1CCS(=O)(=O)C1
|
| 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
|
| ZINC5188799 | 0.556 | 280.5 Da LogP 4.39 TPSA 24.1 | ✓ Ro5 | ✓ Clean |
C(CCCNC1CCCCC1)CCNC1CCCCC1
|
| ZINC2168583 | 0.529 | 237.3 Da LogP 0.16 TPSA 86.6 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)C[C@@H](O)CNC1CCCCC1
|
| ZINC2168584 | 0.529 | 237.3 Da LogP 0.16 TPSA 86.6 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)C[C@H](O)CNC1CCCCC1
|
| 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
|
| ZINC130127586 | 0.515 | 260.4 Da LogP 1.38 TPSA 58.2 | ✓ Ro5 | ✓ Clean |
O=S(=O)(NCCNC1CCCCCC1)C1CC1
|
| ZINC78421079 | 0.515 | 210.3 Da LogP 1.43 TPSA 41.1 | ✓ Ro5 | ✓ Clean |
O=C(NCCNC1CCCCC1)C1CC1
|
| 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
|
| ZINC122239480 | 0.500 | 238.4 Da LogP 2.22 TPSA 41.1 | ✓ Ro5 | ✓ Clean |
O=C(NCCNC1CCCCCC1)C1CCC1
|
| ZINC1560408775 | 0.500 | 338.1 Da LogP -1.54 TPSA 211.3 | 1 viol. | ✓ Clean |
O=C(COP(=O)(O)O)[C@@H](O)/C(O)=C(/O)COP(=O)(O)O
|
| ZINC1560408777 | 0.500 | 338.1 Da LogP -1.54 TPSA 211.3 | 1 viol. | ✓ Clean |
O=C(COP(=O)(O)O)[C@@H](O)/C(O)=C(\O)COP(=O)(O)O
|
| ZINC165485 | 0.500 | 301.8 Da LogP 3.04 TPSA 46.2 | ✓ Ro5 | ✓ Clean |
O=S(=O)(CCNC1CCCCC1)c1ccc(Cl)cc1
|
| 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
|
| ZINC2557605 | 0.500 | 200.4 Da LogP 3.86 TPSA 20.2 | ✓ Ro5 | ✓ Clean |
CC(C)(C)C(O)(C(C)(C)C)C(C)(C)C
|
| ZINC38889906 | 0.500 | 226.4 Da LogP 3.21 TPSA 38.0 | ✓ Ro5 | ✓ Clean |
NCCNC1CCCCCCCCCCC1
|
| ZINC60934954 | 0.500 | 315.9 Da LogP 3.43 TPSA 46.2 | ✓ Ro5 | ✓ Clean |
O=S(=O)(CCNC1CCCCCC1)c1ccc(Cl)cc1
|
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.