Overview
Basic information about this protein and its source genome.
- Accession
- PA4664
- Gene
- prmC PA4664 hemK
- Status
- annotated
- Amino acids
- 276
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 32.773
- Human E-value
- 4.33e-23
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- 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.
MTTICTLLKDSQLPDSPSARLDTELLLAAAMGKPRSFLRTWPERIVPREANERFDDWIARRRNGEPVAYILGHQGFWSLDLEVAPHTLIPRPDTELLVETALATLAADTATVLDLGTGTGAIALALASERPLWTVTAVDRVEEAVALAERNRQRLLLENVEVRRSHWFSALDGRRFRMIVGNPPYIPASDPHLSEGDVRFEPKSALVAGSDGLDDIRQIVAQAPRHLLDEGWLLLEHGYDQGAAVRELLGARGFAGVHTLRDLGGNERITLGQWAC
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
8- GO:0003676 Binding to a nucleic acid.
- GO:0102559 Catalysis of the reaction: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine + H+.
- GO:0036009 Catalysis of the reaction: L-glutaminyl-[protein] + S-adenosyl-L-methionine = N(5)-methyl-L-glutaminyl-[protein] + S-adenosyl-L-homocysteine + H+.
- GO:0032259 The process in which a methyl group is covalently attached to a molecule.
- GO:0006415 The process resulting in the release of a polypeptide chain from the ribosome, usually in response to a termination codon (UAA, UAG, or UGA in the universal genetic code).
- GO:0008276 Catalysis of the transfer of a methyl group (CH3-) to a protein.
- GO:0008168 Catalysis of the transfer of a methyl group to an acceptor molecule.
- GO:0006479 The addition of a methyl group to a protein amino acid. A methyl group is derived from methane by the removal of a hydrogen atom.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 3 | 274 | Hamap | MF_02126 | Release factor glutamine methyltransferase [prmC]. |
| 3 | 274 | InterPro | IPR019874 | Protein-(glutamine-N5) methyltransferase, release factor-specific |
| 112 | 236 | CDD | cd02440 | AdoMet_MTases |
| 12 | 272 | SUPERFAMILY | SSF53335 | S-adenosyl-L-methionine-dependent methyltransferases |
| 12 | 272 | InterPro | IPR029063 | S-adenosyl-L-methionine-dependent methyltransferase superfamily |
| 18 | 276 | NCBIfam | TIGR00536 | HemK family protein methyltransferase |
| 18 | 276 | InterPro | IPR004556 | Methyltransferase HemK-like |
| 94 | 185 | Pfam | PF05175 | Methyltransferase small domain |
| 94 | 185 | InterPro | IPR007848 | Methyltransferase small domain |
| 138 | 158 | Coils | Coil | Coil |
| 22 | 270 | NCBIfam | TIGR03534 | peptide chain release factor N(5)-glutamine methyltransferase |
| 22 | 270 | InterPro | IPR019874 | Protein-(glutamine-N5) methyltransferase, release factor-specific |
| 84 | 275 | FunFam | G3DSA:3.40.50.150:FF:000053 | Release factor glutamine methyltransferase |
| 16 | 72 | Pfam | PF17827 | PrmC N-terminal domain |
| 16 | 72 | InterPro | IPR040758 | Release factor glutamine methyltransferase, N-terminal domain |
| 15 | 272 | PANTHER | PTHR18895 | HEMK METHYLTRANSFERASE |
| 179 | 185 | ProSitePatterns | PS00092 | N-6 Adenine-specific DNA methylases signature. |
| 179 | 185 | InterPro | IPR002052 | DNA methylase, N-6 adenine-specific, conserved site |
| 7 | 82 | Gene3D | G3DSA:1.10.8.10 | - |
| 84 | 275 | Gene3D | G3DSA:3.40.50.150 | Vaccinia Virus protein VP39 |
| 84 | 275 | InterPro | IPR029063 | S-adenosyl-L-methionine-dependent methyltransferase superfamily |
| 7 | 82 | FunFam | G3DSA:1.10.8.10:FF:000141 | Release factor glutamine methyltransferase |
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
PA4664
|
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 |
|---|---|---|---|---|---|---|---|
| 1 | 0.678 | ||||||
| 2 | 0.324 |
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 |
|---|---|---|---|---|---|---|
| MEQ | Q9WYV8 | 160.2 Da LogP -1.08 TPSA 92.4 | ✓ Ro5 | ✓ Clean |
CNC(=O)CC[C@@H](C(=O)O)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 |
|---|---|---|---|---|---|
| ZINC1529737 | 0.714 | 218.2 Da LogP -1.23 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
C[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O
|
| ZINC2384790 | 0.714 | 218.2 Da LogP -1.23 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
C[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O
|
| ZINC2560745 | 0.714 | 218.2 Da LogP -1.23 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
C[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC2560989 | 0.714 | 218.2 Da LogP -1.23 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
C[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC2390999 | 0.655 | 275.3 Da LogP -1.99 TPSA 172.8 | ✓ Ro5 | ✓ Clean |
NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O
|
| ZINC2516115 | 0.613 | 246.3 Da LogP -0.60 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
CC(C)[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O
|
| ZINC13514803 | 0.606 | 347.3 Da LogP -1.88 TPSA 196.1 | 1 viol. | ✓ Clean |
C[C@H](NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=…
|
| ZINC1576202 | 0.600 | 204.2 Da LogP -1.62 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCC(=O)NCC(=O)O)C(=O)O
|
| ZINC3995565 | 0.600 | 204.2 Da LogP -1.62 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
N[C@H](CCC(=O)NCC(=O)O)C(=O)O
|
| ZINC2504764 | 0.594 | 232.2 Da LogP -0.84 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O
|
| ZINC3055005 | 0.591 | 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 | 0.591 | 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 | 0.591 | 204.2 Da LogP -0.63 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC2391099 | 0.586 | 274.3 Da LogP -2.59 TPSA 178.6 | ✓ Ro5 | ✓ Clean |
NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O
|
| ZINC1608689 | 0.576 | 202.3 Da LogP 0.09 TPSA 92.4 | ✓ Ro5 | ✓ Clean |
CCCCNC(=O)CC[C@H](N)C(=O)O
|
| ZINC2045835 | 0.576 | 202.3 Da LogP 0.09 TPSA 92.4 | ✓ Ro5 | ✓ Clean |
CCCCNC(=O)CC[C@@H](N)C(=O)O
|
| ZINC2384788 | 0.576 | 260.3 Da LogP -0.21 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
CC(C)C[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O
|
| ZINC12496578 | 0.571 | 275.3 Da LogP -2.12 TPSA 158.8 | ✓ Ro5 | ✓ Clean |
C[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O
|
| ZINC2556600 | 0.567 | 217.2 Da LogP -1.83 TPSA 135.5 | ✓ Ro5 | ✓ Clean |
C[C@H](NC(=O)[C@@H](N)CCC(N)=O)C(=O)O
|
| ZINC1555366 | 0.565 | 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 | 0.565 | 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 | 0.565 | 232.3 Da LogP 0.15 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1720127 | 0.565 | 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 | 0.565 | 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 | 0.565 | 218.3 Da LogP -0.24 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC13507519 | 0.563 | 234.2 Da LogP -2.26 TPSA 150.0 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCC(=O)N[C@@H](CO)C(=O)O)C(=O)O
|
| ZINC1576203 | 0.563 | 261.2 Da LogP -2.50 TPSA 158.8 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCC(=O)NCC(=O)NCC(=O)O)C(=O)O
|
| ZINC2516116 | 0.563 | 275.3 Da LogP -1.12 TPSA 155.7 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCNC(=O)CC[C@H](N)C(=O)O)C(=O)O
|
| ZINC4545887 | 0.563 | 275.3 Da LogP -1.12 TPSA 155.7 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCNC(=O)CC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC4545888 | 0.563 | 275.3 Da LogP -1.12 TPSA 155.7 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCC(=O)NCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC4545889 | 0.563 | 275.3 Da LogP -1.12 TPSA 155.7 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCCNC(=O)CC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1581634 | 0.552 | 203.2 Da LogP -2.22 TPSA 135.5 | ✓ Ro5 | ✓ Clean |
NC(=O)CC[C@H](N)C(=O)NCC(=O)O
|
| ZINC5500823 | 0.552 | 203.2 Da LogP -2.22 TPSA 135.5 | ✓ Ro5 | ✓ Clean |
NC(=O)CC[C@@H](N)C(=O)NCC(=O)O
|
| ZINC2242694 | 0.545 | 276.2 Da LogP -1.39 TPSA 167.0 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O
|
| ZINC2547582 | 0.545 | 276.2 Da LogP -1.39 TPSA 167.0 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O
|
| ZINC3870040 | 0.545 | 250.3 Da LogP -1.32 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCC(=O)N[C@@H](CS)C(=O)O)C(=O)O
|
| ZINC3870041 | 0.545 | 250.3 Da LogP -1.32 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCC(=O)N[C@H](CS)C(=O)O)C(=O)O
|
| ZINC3870042 | 0.545 | 250.3 Da LogP -1.32 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
N[C@H](CCC(=O)N[C@@H](CS)C(=O)O)C(=O)O
|
| ZINC3870043 | 0.545 | 250.3 Da LogP -1.32 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
N[C@H](CCC(=O)N[C@H](CS)C(=O)O)C(=O)O
|
| ZINC3872193 | 0.545 | 240.2 Da LogP -1.86 TPSA 146.8 | ✓ Ro5 | ✓ Clean |
N[C@H](CCC(=O)NCS(=O)(=O)O)C(=O)O
|
| ZINC4096970 | 0.545 | 405.4 Da LogP -2.04 TPSA 233.4 | 1 viol. | ✓ Clean |
N[C@@H](CCC(=O)N[C@@H](CCC(=O)N[C@@H](CCC(=O)O)…
|
| ZINC4545890 | 0.545 | 276.2 Da LogP -1.39 TPSA 167.0 | ✓ Ro5 | ✓ Clean |
N[C@H](CCC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O
|
| ZINC4545891 | 0.545 | 276.2 Da LogP -1.39 TPSA 167.0 | ✓ Ro5 | ✓ Clean |
N[C@H](CCC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O
|
| ZINC2560992 | 0.531 | 275.3 Da LogP -1.99 TPSA 172.8 | ✓ Ro5 | ✓ Clean |
NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(=O)O)C(=O)O
|
| ZINC12954078 | 0.529 | 222.2 Da LogP 0.82 TPSA 92.4 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCC(=O)Nc1ccccc1)C(=O)O
|
| ZINC12954085 | 0.529 | 222.2 Da LogP 0.82 TPSA 92.4 | ✓ Ro5 | ✓ Clean |
N[C@H](CCC(=O)Nc1ccccc1)C(=O)O
|
| ZINC2106542 | 0.519 | 245.3 Da LogP 1.99 TPSA 100.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCCCCCCC(=O)O)C(=O)O
|
| ZINC2106543 | 0.519 | 245.3 Da LogP 1.99 TPSA 100.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCCCCCCCC(=O)O)C(=O)O
|
| ZINC2108713 | 0.519 | 217.3 Da LogP 1.21 TPSA 100.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCCCCC(=O)O)C(=O)O
|
| ZINC2108714 | 0.519 | 217.3 Da LogP 1.21 TPSA 100.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCCCCCC(=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.