Protein profile

KP13_02398

Phosphoadenosine phosphosulfate reductase

Genome: KpKP13

Gene: cysH AHE42969.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GSB7
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Amino acids 244
Annotations 6
Features 17
PDB binders 2
Druggability 0.797

Overview

Basic information about this protein and its source genome.

Accession
KP13_02398
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
cysH AHE42969.1
Status
annotated
Amino acids
244
Structure source
AlphaFold + ColabFold
EC
1.8.4.8
GO
GO:0004604 Catalysis of the reaction: adenosine 3',5'-diphosphate + H+ + sulfite + thioredoxin disulfide = 3'-phospho-5'-adenylyl sulfate + thioredoxin. Thioredoxin disulfide is the oxidized form of thioredoxin; 3'-phosphoadenosine 5'-phosphosulfate is also known as PAPS. GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. GO:0019379 The pathway by which inorganic sulfate is processed and incorporated into sulfated compounds, where the phosphoadenylyl sulfate reduction step is catalyzed by the enzyme phosphoadenylyl-sulfate reductase (thioredoxin) (EC:1.8.4.8). GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0070814 The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Cytoplasmic
ColabFold pLDDT
91.51

Selected Druggability evidence

AlphaFold / UniProt model

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 0.797
Structure A0A0H3GSB7
Pocket Pocket 13
P2Rank 0.96
Structure A0A0H3GSB7
Pocket Pocket 1
ColabFold model
FPocket 0.702 · Pocket 16
P2Rank 0.953 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 119 / 4744 genomes with a hit
Normalized 0.025

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

5
  • GO:0004604 Catalysis of the reaction: adenosine 3',5'-diphosphate + H+ + sulfite + thioredoxin disulfide = 3'-phospho-5'-adenylyl sulfate + thioredoxin. Thioredoxin disulfide is the oxidized form of thioredoxin; 3'-phosphoadenosine 5'-phosphosulfate is also known as PAPS.
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
  • GO:0019379 The pathway by which inorganic sulfate is processed and incorporated into sulfated compounds, where the phosphoadenylyl sulfate reduction step is catalyzed by the enzyme phosphoadenylyl-sulfate reductase (thioredoxin) (EC:1.8.4.8).
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0070814 The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records
Show feature table
Start End DB Term Name
49 213 CDD cd01713 PAPS_reductase
49 213 InterPro IPR002500 Phosphoadenosine phosphosulphate reductase
33 243 NCBIfam TIGR00434 phosophoadenylyl-sulfate reductase
33 243 InterPro IPR004511 Phosphoadenosine phosphosulphate/adenosine 5'-phosphosulphate reductase
48 219 Pfam PF01507 Phosphoadenosine phosphosulfate reductase family
48 219 InterPro IPR002500 Phosphoadenosine phosphosulphate reductase
21 208 SUPERFAMILY SSF52402 Adenine nucleotide alpha hydrolases-like
5 243 Hamap MF_00063 Adenosine 5'-phosphosulfate reductase [cysH].
5 243 InterPro IPR004511 Phosphoadenosine phosphosulphate/adenosine 5'-phosphosulphate reductase
7 244 PIRSF PIRSF000857 PAPS_reductase
7 244 InterPro IPR004511 Phosphoadenosine phosphosulphate/adenosine 5'-phosphosulphate reductase
2 216 FunFam G3DSA:3.40.50.620:FF:000043 Phosphoadenosine phosphosulfate reductase
19 243 PANTHER PTHR46509 PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE
21 242 NCBIfam TIGR02057 phosphoadenosine phosphosulfate reductase
21 242 InterPro IPR011800 Phosphoadenosine phosphosulphate reductase CysH
2 216 Gene3D G3DSA:3.40.50.620 HUPs
2 216 InterPro IPR014729 Rossmann-like alpha/beta/alpha sandwich fold

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 + 2

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GSB7
AlphaFold — — full sequence — Viewing
ColabFold KP13_02398
ColabFold — — full sequence — Loaded
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
13 0.797

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 26.49 0.914

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.

52 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
A3P
2OQ2
P18408 427.2 Da LogP -1.75 TPSA 232.6 2 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
ADX
2GOY
O05927 427.3 Da LogP -2.04 TPSA 229.4 1 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…

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.