Overview
Basic information about this protein and its source genome.
- Accession
- PA5290
- Gene
- PA5290
- Status
- annotated
- Amino acids
- 497
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- 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.
MSLAIVHSRAQVGVEAPCVSVEAHLANGLPSLTLVGLPETAVRESKDRVRSALLNAGFDFPARRITLNLAPADLPKDGGRFDLAIALGILAASGQLPGTALDGLECLGELALSGAIRPVRGVLPAALAARDARRVLVVPKENAEEASLASGLTVFAVDHLLEIAGHLSGQAPLPPYQARGLLRAPFPYPDLAEVQGQAAAKRALLVAAAGAHNLLLSGPPGTGKTLLASRLPGLLPALDEDEALEVAAIHSVASHVPLRHWPQRPFRQPHHSASAPALVGGGSRPQPGEITLAHQGVLFLDELPEFERKVLEVLREPLESGEIVIARANGRVRFPARFQLVAAMNPCPCGYLGDPSGRCRCTPEQVQRYRGKLSGPLLDRIDLHVSVLRESTSLQPGHGETATAEVSERVGAARQRQLARQGCANAHLDLQAMHRNCALAEADRRWLEAAGERLELSLRALHRILKVARTLADLERIDAIERRHLAEALQYRAMTST
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
4- GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
- GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
- GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
- GO:0032508 OBSOLETE. The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating a region of unpaired single strands.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 21 | 142 | Pfam | PF13541 | Subunit ChlI of Mg-chelatase |
| 191 | 497 | Gene3D | G3DSA:3.40.50.300 | - |
| 191 | 497 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 286 | 390 | ProSiteProfiles | PS50051 | MCM family domain profile. |
| 286 | 390 | InterPro | IPR001208 | MCM domain |
| 6 | 492 | NCBIfam | TIGR00368 | YifB family Mg chelatase-like AAA ATPase |
| 6 | 492 | InterPro | IPR004482 | Mg chelatase-related protein |
| 210 | 391 | SMART | SM00382 | AAA_5 |
| 210 | 391 | InterPro | IPR003593 | AAA+ ATPase domain |
| 190 | 390 | Pfam | PF01078 | Magnesium chelatase, subunit ChlI |
| 190 | 390 | InterPro | IPR000523 | Magnesium chelatase ChlI-like, catalytic domain |
| 187 | 492 | SUPERFAMILY | SSF52540 | P-loop containing nucleoside triphosphate hydrolases |
| 187 | 492 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 402 | 492 | Pfam | PF13335 | Magnesium chelatase, subunit ChlI C-terminal |
| 402 | 492 | InterPro | IPR025158 | Mg chelatase-related protein, C-terminal domain |
| 340 | 352 | PRINTS | PR01657 | Mini-chromosome maintenance (MCM) protein family signature |
| 340 | 352 | InterPro | IPR001208 | MCM domain |
| 288 | 302 | PRINTS | PR01657 | Mini-chromosome maintenance (MCM) protein family signature |
| 288 | 302 | InterPro | IPR001208 | MCM domain |
| 209 | 224 | PRINTS | PR01657 | Mini-chromosome maintenance (MCM) protein family signature |
| 209 | 224 | InterPro | IPR001208 | MCM domain |
| 316 | 329 | PRINTS | PR01657 | Mini-chromosome maintenance (MCM) protein family signature |
| 316 | 329 | InterPro | IPR001208 | MCM domain |
| 13 | 168 | Gene3D | G3DSA:3.30.230.10 | - |
| 13 | 168 | InterPro | IPR014721 | Ribosomal protein S5 domain 2-type fold, subgroup |
| 19 | 491 | PANTHER | PTHR32039 | MAGNESIUM-CHELATASE SUBUNIT CHLI |
| 19 | 491 | InterPro | IPR045006 | Magnesium-chelatase subunit ChlI-like |
| 8 | 169 | SUPERFAMILY | SSF54211 | Ribosomal protein S5 domain 2-like |
| 8 | 169 | InterPro | IPR020568 | Ribosomal protein S5 domain 2-type fold |
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
PA5290
|
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 | 0.76 | ||||||
| 1 | 0.6 |