Protein profile

PA1068

heat shock protein

Genome: NC_002516.2

Gene: PA1068 Structure source: AlphaFold UniProt Q9I4Q6
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Amino acids 636
Annotations 8
Features 28
PDB binders 4
Druggability 0.675

Overview

Basic information about this protein and its source genome.

Accession
PA1068
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1068
Status
annotated
Amino acids
636
Structure source
AlphaFold
GO
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. 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:0140662 Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. GO:0051082 Binding to an unfolded protein. GO:0006974 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
29.885
Human E-value
3.48e-13
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 0.675
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MAESRTGPLACERTPFIERLDRDMQSSFPQSNTPQIRRAGVDLNGVMSVLSKHLYSTPTVALRELVQNAHDSILRRRLEQPDWQGPSRIEVIGDSASNTVRIVDTGAGLTEHEIHAYLATVGVGYTRGLRQSGHEDSGLIGMFGLGFLSAFVLARRVSVRTTSYQQPELGFCYVSSNAEQYSVTPMPARPVGTEITLELQDEYSALTQAARLREILERYCVLLREPIHVGGDAQSINPEPPPWRLAADAALHPLQRQRRDLEFAARFEHDFEPICCLPVRPDERVDVQGLLWIQDGGTYGTSDNRNLSVFLRGMLLDDDARDLLPSWAGFVGGVIESNRLTPTASREDLQRDDHYAAIQHALAEALIAGLGEVARQQPEAWRRVLLRHNEALLGAALCDERLFALMMDSLRVPTSQGDLPASELLSRGAVHVLLDNDSGFEEMLFRAMGVPVAHGNRYAVVPFLRRWAQAKGMRLVELGTEQGNRQLFRLDRLPEHETGWLAEHLGGAEEQLVIARFSPEELPLVVVPDRDAELKRRLEDDEADKRISTAALRLARQFTRKLDNRQPSRLYVNLDNPAVQALLAAVGEERDEAAHAALLLRSFKVIIAGQGRGQPATSLNQALAGLADSVKRLLEQ

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

8
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • 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:0140662 Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
  • GO:0051082 Binding to an unfolded protein.
  • GO:0006974 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
  • GO:0006457 The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
  • GO:0009408 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.

Sequence Features

Domain/signature hits from InterPro and related databases.

28 records
Show feature table
Start End DB Term Name
43 376 PANTHER PTHR11528 HEAT SHOCK PROTEIN 90 FAMILY MEMBER
43 376 InterPro IPR001404 Heat shock protein Hsp90 family
137 154 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
24 230 FunFam G3DSA:3.30.565.10:FF:000418 Probable heat shock protein (Hsp90 family)
256 479 SUPERFAMILY SSF54211 Ribosomal protein S5 domain 2-like
256 479 InterPro IPR020568 Ribosomal protein S5 domain 2-type fold
44 223 CDD cd16927 HATPase_Hsp90-like
44 223 InterPro IPR020575 Heat shock protein Hsp90, N-terminal
155 636 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
40 231 Gene3D G3DSA:3.30.565.10 -
40 231 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
258 406 Gene3D G3DSA:3.30.230.80 -
56 78 PRINTS PR00775 90kDa heat shock protein signature
56 78 InterPro IPR020575 Heat shock protein Hsp90, N-terminal
140 162 PRINTS PR00775 90kDa heat shock protein signature
140 162 InterPro IPR020575 Heat shock protein Hsp90, N-terminal
209 227 PRINTS PR00775 90kDa heat shock protein signature
209 227 InterPro IPR020575 Heat shock protein Hsp90, N-terminal
191 208 PRINTS PR00775 90kDa heat shock protein signature
191 208 InterPro IPR020575 Heat shock protein Hsp90, N-terminal
58 166 Pfam PF13589 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
36 232 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
36 232 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
300 377 Pfam PF00183 Hsp90 protein
300 377 InterPro IPR001404 Heat shock protein Hsp90 family
15 632 PIRSF PIRSF002583 HSP90_HTPG
15 632 InterPro IPR001404 Heat shock protein Hsp90 family
1 136 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA1068
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 0.675
7 0.284
8 0.272

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.

154 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
ACP
4X9L
Q07078 505.2 Da LogP -1.52 TPSA 269.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
ALF
4IYN
A8WFV1 103.0 Da LogP 1.30 TPSA 0.0 ✓ Ro5 ✓ Clean F[Al-](F)(F)F
ANP
6D14
A8WFV1 506.2 Da LogP -2.06 TPSA 281.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
BEF
4J0B
A8WFV1 66.0 Da LogP 0.88 TPSA 0.0 ✓ Ro5 ✓ Clean [Be-](F)(F)F

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.