Protein profile

KP13_00214

Serine acetyltransferase

Genome: KpKP13

Gene: AHE42127.1 cysE Structure source: Experimental + ColabFold UniProt A6TFK2

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Amino acids 273

Annotations 4

Features 19

PDB binders 3

Druggability 0.415

Overview

Basic information about this protein and its source genome.

Accession: KP13_00214
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE42127.1 cysE
Status: annotated
Amino acids: 273
Structure source: Experimental + ColabFold

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. GO:0009001 Catalysis of the reaction: L-serine + acetyl-CoA = O-acetyl-L-serine + CoA. GO:0006535 OBSOLETE. The chemical reactions and pathways resulting in the formation of cysteine from L- serine.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 95.604
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 95.44

Selected Druggability evidence

PDB experimental structure

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 0.415

Structure 6JVU

Pocket Pocket 4

P2Rank 0.061

Structure 6JVU

Pocket Pocket 1

ColabFold model

FPocket 0.541 · Pocket 14

P2Rank 0.19 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 188 / 4744 genomes with a hit

Normalized 0.04

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
GO:0009001 Catalysis of the reaction: L-serine + acetyl-CoA = O-acetyl-L-serine + CoA.
GO:0006535 OBSOLETE. The chemical reactions and pathways resulting in the formation of cysteine from L- serine.

Sequence Features

Domain/signature hits from InterPro and related databases.

19 records

Show feature table

Start	End	DB	Term	Name
9	113	SMART	SM00971	SATase_N_2_a
9	113	InterPro	IPR010493	Serine acetyltransferase, N-terminal
143	264	FunFam	G3DSA:2.160.10.10:FF:000002	Serine acetyltransferase
202	230	ProSitePatterns	PS00101	Hexapeptide-repeat containing-transferases signature.
202	230	InterPro	IPR018357	Hexapeptide transferase, conserved site
9	113	Pfam	PF06426	Serine acetyltransferase, N-terminal
1	142	FunFam	G3DSA:1.10.3130.10:FF:000001	Acetyltransferase
1	142	Gene3D	G3DSA:1.10.3130.10	serine acetyltransferase, domain 1
1	142	InterPro	IPR042122	Serine acetyltransferase, N-terminal domain superfamily
140	240	CDD	cd03354	LbH_SAT
140	240	InterPro	IPR045304	Serine acetyltransferase, LbH domain
82	242	NCBIfam	TIGR01172	serine O-acetyltransferase
82	242	InterPro	IPR005881	Serine O-acetyltransferase
193	226	Pfam	PF00132	Bacterial transferase hexapeptide (six repeats)
193	226	InterPro	IPR001451	Hexapeptide repeat
4	260	SUPERFAMILY	SSF51161	Trimeric LpxA-like enzymes
4	260	InterPro	IPR011004	Trimeric LpxA-like superfamily
4	258	PANTHER	PTHR42811	SERINE ACETYLTRANSFERASE
143	273	Gene3D	G3DSA:2.160.10.10	Hexapeptide repeat proteins

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...

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Structural evidence

1 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
PDB 6JVU	X-ray	20.00 Å	-	—	PDBe RCSB PDBj File	Viewing
ColabFold KP13_00214	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
80				0.925
1				0.867

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	Score	Probability
1	36.79	0.956
2	31.99	0.941
3	31.4	0.939
4	28.32	0.924
5	26.2	0.911

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
14				0.541
2				0.358

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				2.64	0.077
2				2.35	0.061

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.

53 records

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
15P	4HZD	A0A0F6AR69	1529.8 Da LogP 0.17 TPSA 334.1	2 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO…`
OAS	4ZU1	P29847	147.1 Da LogP -1.04 TPSA 89.6	✓ Ro5	✓ Clean	`CC(=O)OC[C@@H](C(=O)O)N`
PG5	3GVD	A0A2U2H3H7	178.2 Da LogP 0.31 TPSA 36.9	✓ Ro5	✓ Clean	`COCCOCCOCCOC`

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
ZINC1580161	1.000	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118	1.000	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257	1.000	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654	1.000	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44076059	1.000	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101	1.000	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5997860	1.000	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC575419714	0.727	312.4 Da LogP 0.42 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCSCCOCCOCCO`
ZINC115163232	0.700	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCO`
ZINC258837490	0.700	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCCO`
ZINC1692489	0.688	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC4530388	0.688	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5701172	0.688	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861	0.688	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC1706207	0.583	202.2 Da LogP 0.32 TPSA 69.7	✓ Ro5	✓ Clean	`CC(=O)OCC(COC(C)=O)C(C)=O`
ZINC34111591	0.583	207.3 Da LogP -1.06 TPSA 62.2	✓ Ro5	✓ Clean	`COCCOCCN(CCO)CCO`
ZINC100017163	0.553	213.3 Da LogP 0.71 TPSA 99.2	✓ Ro5	✓ Clean	`C/C=C/CC(=N)NCCC[C@H](N)C(=O)O`
ZINC19796052	0.553	219.2 Da LogP -1.73 TPSA 156.9	✓ Ro5	✓ Clean	`N/C(=N\[N+](=O)[O-])NCCC[C@H](N)C(=O)O`
ZINC21982226	0.553	219.2 Da LogP -1.73 TPSA 156.9	✓ Ro5	✓ Clean	`N/C(=N\[N+](=O)[O-])NCCC[C@@H](N)C(=O)O`
ZINC34764844	0.550	206.3 Da LogP 1.09 TPSA 36.9	✓ Ro5	✓ Clean	`CCCOCCOCCOCCOC`
ZINC2383745924	0.542	398.5 Da LogP -0.01 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCC(CO)COCCOCCOCCOC`
ZINC5131766	0.538	224.3 Da LogP -1.26 TPSA 92.4	✓ Ro5	✓ Clean	`N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)O`
ZINC1529646	0.526	290.3 Da LogP -1.78 TPSA 185.8	1 viol.	✓ Clean	`N=C(NCCC[C@H](N)C(=O)O)N[C@@H](CC(=O)O)C(=O)O`
ZINC2043460	0.526	214.3 Da LogP -0.52 TPSA 111.2	✓ Ro5	✓ Clean	`C=CCNC(=N)NCCC[C@H](N)C(=O)O`
ZINC3105913	0.526	240.2 Da LogP 1.22 TPSA 54.0	✓ Ro5	✓ Clean	`COCCOCP(C)(=O)COCCOC`
ZINC115086873	0.524	209.2 Da LogP -1.08 TPSA 83.2	✓ Ro5	✓ Clean	`NOCCOCCOCCOCCO`
ZINC140264883	0.524	223.3 Da LogP -0.43 TPSA 72.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCON`
ZINC146143823	0.524	237.3 Da LogP -1.00 TPSA 83.2	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCO`
ZINC1565503710	0.524	254.3 Da LogP -0.03 TPSA 57.2	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCS`
ZINC1730666	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CSC[C@H](N)C(=O)O)C(=O)O`
ZINC1730667	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CSC[C@H](N)C(=O)O)C(=O)O`
ZINC1730669	0.524	208.2 Da LogP -1.46 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CSC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055005	0.524	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	0.524	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	0.524	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC33358855	0.524	207.3 Da LogP -0.36 TPSA 62.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCN`
ZINC38917157	0.524	210.3 Da LogP -0.04 TPSA 47.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCS`
ZINC44583772	0.524	356.5 Da LogP 0.66 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCS`
ZINC5024003	0.524	251.3 Da LogP -0.34 TPSA 72.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCN`
ZINC575432090	0.524	355.4 Da LogP -0.38 TPSA 99.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCON`
ZINC575432265	0.524	399.5 Da LogP -0.36 TPSA 109.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCON`
ZINC71254558	0.524	444.6 Da LogP 0.70 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC83253921	0.524	369.5 Da LogP -0.95 TPSA 110.9	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC83253930	0.524	224.3 Da LogP 0.61 TPSA 36.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCS`
ZINC83253936	0.524	383.5 Da LogP -0.29 TPSA 99.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCN`
ZINC90556279	0.524	295.4 Da LogP -0.33 TPSA 81.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCN`
ZINC90556287	0.524	268.4 Da LogP 0.63 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCS`
ZINC90741446	0.524	386.5 Da LogP 0.02 TPSA 84.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC90741447	0.524	298.4 Da LogP -0.01 TPSA 66.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCS`
ZINC96503353	0.524	471.6 Da LogP -0.26 TPSA 118.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCN`

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.