Protein target profile

KP13_01654

Dihydrodipicolinate synthase

Genome: KpKP13 Gene: AHE43824.1 dapA 3D evidence: AlphaFold DB model + ColabFold model UniProt W8UXW6

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Length 356

Pocket druggability 0.428

Direct ligand evidence 0 61 total records

Functional annotation 1 EC 3 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Moderate predicted binding pocket FPocket selected-pocket score 0.43. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.84. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: No hit
Gut microbiome similarity: 0.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 85.84 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.428

Structure W8UXW6

Pocket Pocket 17

P2Rank 0.841

Structure W8UXW6

Pocket Pocket 1

ColabFold model

FPocket 0.489 · Pocket 7

P2Rank 0.872 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 34 / 4744 genomes with a hit

Prevalence 0.7%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt W8UXW6

Sequence

Primary amino-acid sequence viewer.

MKPPTGGFFVSVLSLSDTIPASLTPRRFSVNSSLTVNFSFVPGQNDRVLLLSNGLSAQPAGGIMFTGLCAFPLTPLHQQDFDEKAFIRILARLTDAGVDSLGILGSTGSYAYLSREQRRRVVQVAKAHAGSIPMMVGVGAIATNEVLRLVEDAQEAGADALLLPMMSYQPLSAEEIFAFYEEVCRHVSVPVCLYDNPRTTHVMLADELQGRIAALPAIASIKIPGLPAPQASERVAALRQHLPSRVTLGVSGDAWATAGLQAGCEAWYSVCGGLFPRFSLALVRAIRSGDVAQTAALNEQLAPLWRCFDRYGGSLRVIASAAAMLGLCDPDSLPRPLLSLGEEACREVASALRGLA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 3 GO

Enzyme Commission (EC)

4.3.3.7

Gene Ontology (GO)

GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0008840 Catalysis of the reaction: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O + H+.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

21 records

Show feature table

Start	End	DB	Term	Name
16	20	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
65	352	Pfam	PF00701	Dihydrodipicolinate synthetase family
65	352	InterPro	IPR002220	DapA-like
1	20	Phobius	SIGNAL_PEPTIDE	Signal peptide region
64	355	SUPERFAMILY	SSF51569	Aldolase
70	352	CDD	cd00408	DHDPS-like
132	150	PRINTS	PR00146	Dihydrodipicolinate synthase signature
132	150	InterPro	IPR002220	DapA-like
189	206	PRINTS	PR00146	Dihydrodipicolinate synthase signature
189	206	InterPro	IPR002220	DapA-like
97	118	PRINTS	PR00146	Dihydrodipicolinate synthase signature
97	118	InterPro	IPR002220	DapA-like
64	356	SMART	SM01130	DHDPS_2
64	356	InterPro	IPR002220	DapA-like
61	353	PANTHER	PTHR12128	DIHYDRODIPICOLINATE SYNTHASE
61	353	InterPro	IPR002220	DapA-like
5	15	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
21	356	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
64	356	Gene3D	G3DSA:3.20.20.70	Aldolase class I
64	356	InterPro	IPR013785	Aldolase-type TIM barrel
1	4	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #17

0.428

Likely same site as P2Rank 1 2.3 Å 20 shared residues 95% of smaller site

Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.841

Likely same site as FPocket 17 2.3 Å 20 shared residues 95% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.035

Show in viewer

Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_W8UXW6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01654	ColabFold	—	—	full sequence	—	Loaded

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.

61 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 11 records from similar proteins

Structural ligands 11 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2KT PDB via homolog 102.1 Da · LogP 0.05 · TPSA 54.4 Open detail RCSB PDB

3VN PDB via homolog Detail RCSB PDB

GXP PDB via homolog Detail RCSB PDB

GXT PDB via homolog Detail RCSB PDB

GXV PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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
2KT RCSB PDB	3TDF	D0CFC3	102.1 Da LogP 0.05 TPSA 54.4	✓ Ro5	✓ Clean	`CCC(=O)C(=O)O`
3VN RCSB PDB	5F1U	Q9PPB4	318.4 Da LogP -0.41 TPSA 178.7	1 viol.	✓ Clean	`C(CCN)C[C@@](CC[C@](CCCCN)(C(=O)O)N)(C(=O)O)N`
GXP RCSB PDB	4OE7	P75682	146.1 Da LogP -1.41 TPSA 91.7	✓ Ro5	✓ Clean	`C([C@@H](C=O)O)C(=O)C(=O)O`
GXT RCSB PDB	4OE7	P75682	58.0 Da LogP -0.62 TPSA 34.1	✓ Ro5	✓ Clean	`C(=O)C=O`
GXV RCSB PDB	4PTN	P75682	90.1 Da LogP -1.46 TPSA 57.5	✓ Ro5	✓ Clean	`C([C@@H](C=O)O)O`
KDG RCSB PDB	4ONV	P75682	178.1 Da LogP -2.26 TPSA 115.1	✓ Ro5	✓ Clean	`C([C@@H]([C@@H](CO)O)O)C(=O)C(=O)O`
LYZ RCSB PDB	3TCE	D0CFC3	162.2 Da LogP -1.50 TPSA 109.6	✓ Ro5	✓ Clean	`C(C[C@@H](C(=O)O)N)[C@H](CN)O`
MLT RCSB PDB	3NA8	Q9I6R5	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
OXL RCSB PDB	3U8G	D0CFC3	88.0 Da LogP -3.51 TPSA 80.3	✓ Ro5	✓ Clean	`C(=O)(C(=O)[O-])[O-]`
PYR RCSB PDB	3RK8	D0CFC3	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=O)O`
RSH RCSB PDB	3NEV	P75682	180.2 Da LogP -2.46 TPSA 118.2	✓ Ro5	✓ Clean	`C([C@H]([C@@H](CO)O)O)[C@@H](C(=O)O)O`

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
ZINC2562361 ZINC	0.739	238.2 Da LogP -3.53 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)C(=O)C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC3870003 ZINC	0.739	238.2 Da LogP -3.53 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)C(=O)C[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC8551322 ZINC	0.739	238.2 Da LogP -3.53 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)C(=O)C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC8551323 ZINC	0.739	238.2 Da LogP -3.53 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)C(=O)C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC8551324 ZINC	0.739	238.2 Da LogP -3.53 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)C(=O)C[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC2562359 ZINC	0.708	268.2 Da LogP -4.17 TPSA 175.7	1 viol.	✓ Clean	`O=C(O)C(=O)C[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)[…`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC71773889 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@H](O)C(=O)O`
ZINC71773890 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC71773891 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC5113885 ZINC	0.630	307.3 Da LogP -2.32 TPSA 179.1	1 viol.	✓ Clean	`N[C@@H](CC[C@H](O)CNC[C@H](O)CC[C@H](N)C(=O)O)C…`
ZINC5113891 ZINC	0.630	307.3 Da LogP -2.32 TPSA 179.1	1 viol.	✓ Clean	`N[C@@H](CC[C@@H](O)CNC[C@H](O)CC[C@H](N)C(=O)O)…`
ZINC14686440 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC13398039 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC12506611 ZINC	0.571	201.1 Da LogP 0.10 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](CC[C@@H](O)C(F)(F)F)C(=O)O`
ZINC12506613 ZINC	0.571	201.1 Da LogP 0.10 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](CC[C@@H](O)C(F)(F)F)C(=O)O`
ZINC12506615 ZINC	0.571	201.1 Da LogP 0.10 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](CC[C@H](O)C(F)(F)F)C(=O)O`
ZINC12506617 ZINC	0.571	201.1 Da LogP 0.10 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](CC[C@H](O)C(F)(F)F)C(=O)O`
ZINC146315135 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315336 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@](O)(CC(=O)O)C(=O)O`
ZINC1850353 ZINC	0.556	206.1 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC(O)(CC(=O)O)CC(=O)O`
ZINC3055005 ZINC	0.542	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 ZINC	0.542	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 ZINC	0.542	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC96301090 ZINC	0.536	200.2 Da LogP 0.07 TPSA 89.3	✓ Ro5	✓ Clean	`N[C@H](CC[C@@H](N)C(F)(F)F)C(=O)O`
ZINC1577651 ZINC	0.526	234.2 Da LogP -0.66 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C[C@H](C(=O)O)[C@@H](CC(=O)O)C(=O)O`
ZINC1577652 ZINC	0.526	234.2 Da LogP -0.66 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C[C@@H](C(=O)O)[C@@H](CC(=O)O)C(=O)O`
ZINC1577653 ZINC	0.526	234.2 Da LogP -0.66 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C[C@H](C(=O)O)[C@H](CC(=O)O)C(=O)O`
ZINC13398014 ZINC	0.522	220.2 Da LogP -1.07 TPSA 110.1	✓ Ro5	✓ Clean	`COC(=O)CC(O)(CC(=O)OC)C(=O)O`
ZINC3861629 ZINC	0.522	206.1 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C(O)(CC(=O)O)CC(=O)O`
ZINC1555366 ZINC	0.520	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 ZINC	0.520	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 ZINC	0.520	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 ZINC	0.520	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 ZINC	0.520	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 ZINC	0.520	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC14418070 ZINC	0.515	291.3 Da LogP -1.29 TPSA 158.9	1 viol.	✓ Clean	`N[C@H](CCCCNC[C@@H](O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC14418072 ZINC	0.515	291.3 Da LogP -1.29 TPSA 158.9	1 viol.	✓ Clean	`N[C@H](CCCCNC[C@H](O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC257547123 ZINC	0.515	291.3 Da LogP -1.29 TPSA 158.9	1 viol.	✓ Clean	`N[C@@H](CC[C@@H](O)CNCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC4523370 ZINC	0.515	309.3 Da LogP -4.03 TPSA 184.6	1 viol.	✓ Clean	`CC(=O)N[C@@H]([C@H](O)[C@H](O)[C@H](O)CO)[C@H](…`
ZINC4523373 ZINC	0.515	309.3 Da LogP -4.03 TPSA 184.6	1 viol.	✓ Clean	`CC(=O)N[C@@H]([C@@H](O)CC(=O)C(=O)O)[C@H](O)[C@…`
ZINC4523376 ZINC	0.515	309.3 Da LogP -4.03 TPSA 184.6	1 viol.	✓ Clean	`CC(=O)N[C@H]([C@@H](O)CC(=O)C(=O)O)[C@H](O)[C@H…`
ZINC5113220 ZINC	0.515	291.3 Da LogP -1.29 TPSA 158.9	1 viol.	✓ Clean	`N[C@@H](CCCCNC[C@@H](O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC5113224 ZINC	0.515	291.3 Da LogP -1.29 TPSA 158.9	1 viol.	✓ Clean	`N[C@@H](CC[C@H](O)CNCCCC[C@@H](N)C(=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.