KpKP13 Protein target profile

N-acetylmuramoyl-L-alanine amidase amiD

Accession: KP13_04238

Gene: amiD AHE45469.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GKW4

Export view

Length 276

Pocket druggability (P2Rank · AlphaFold DB model) 0.328

Direct ligand evidence 0 48 total records

Functional annotation 1 EC 5 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. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.40. This supports review but is not experimental validation. 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: 1.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 76.364 Higher values support similarity to known essential genes.
DEG E-value: 1.82e-154 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 94.77 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.328

Structure A0A0H3GKW4

Pocket Pocket 1

Druggability (FPocket) 0.401

Structure A0A0H3GKW4

Pocket Pocket 8

ColabFold model

P2Rank 0.411 · Pocket 1

FPocket 0.448 · Pocket 3

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 85 / 4744 genomes with a hit

Prevalence 1.8%

Sequence

Primary amino-acid sequence viewer.

MKRMMRIVLLALLLTGCAGEKGIIDRDGYQLDTRHPAQAAYPRIKVLVIHYTADNFDVSLATLTDKEVSSHYLIPEQPPRYQHKPRIWQLVPEEDLAWHAGVSYWRGSTRINDTSIGIELENRGWQKTAGVKSFTPFHPEQIAALIPLARDIIARYHIAPQNVVAHADIAPQRKDDPGPLFPWQQLAQQGIGAWPDEQRVAFYLNGRPASEPVDPEIVLDLLSRYGYQVTPEMTPAQKKRVIIAFQMHFRPQRWDGVADAQTEAIAEALLEKYGQG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Subcellular localization

Localization: Unknown

Enzyme Commission (EC)

3.5.1.28

Gene Ontology (GO)

GO:0009253 The chemical reactions and pathways resulting in the breakdown of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
GO:0008745 Catalysis of the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain bacterial cell-wall glycopeptides.
GO:0019867 The external membrane of Gram-negative bacteria or certain organelles such as mitochondria and chloroplasts; freely permeable to most ions and metabolites.
GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
GO:0009254 The continual breakdown and regeneration of peptidoglycan required to maintain the bacterial cell wall. Peptidoglycans consist of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
7	14	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
1	19	SignalP_EUK	SignalP-noTM	SignalP-noTM
42	179	Pfam	PF01510	N-acetylmuramoyl-L-alanine amidase
42	179	InterPro	IPR002502	N-acetylmuramoyl-L-alanine amidase domain
43	180	CDD	cd06583	PGRP
43	180	InterPro	IPR002502	N-acetylmuramoyl-L-alanine amidase domain
36	269	PANTHER	PTHR30417	N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID
32	178	SMART	SM00644	ami_2
32	178	InterPro	IPR002502	N-acetylmuramoyl-L-alanine amidase domain
42	192	FunFam	G3DSA:3.40.80.10:FF:000003	N-acetylmuramoyl-L-alanine amidase
43	192	Gene3D	G3DSA:3.40.80.10	-
43	192	InterPro	IPR036505	N-acetylmuramoyl-L-alanine amidase/PGRP domain superfamily
1	20	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
1	6	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
16	42	Gene3D	G3DSA:6.20.370.150	-
23	194	SUPERFAMILY	SSF55846	N-acetylmuramoyl-L-alanine amidase-like
23	194	InterPro	IPR036505	N-acetylmuramoyl-L-alanine amidase/PGRP domain superfamily
198	273	SUPERFAMILY	SSF47090	PGBD-like
198	273	InterPro	IPR036365	PGBD-like superfamily
1	19	Phobius	SIGNAL_PEPTIDE	Signal peptide region
20	276	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
193	276	Gene3D	G3DSA:1.10.101.10	-
193	276	InterPro	IPR036366	PGBD superfamily
15	19	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	17	ProSiteProfiles	PS51257	Prokaryotic membrane lipoprotein lipid attachment site profile.

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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 · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.328

Likely same site as FPocket 1 2.4 Å 12 shared residues 86% of smaller site

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.013

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #8

0.401

Show in viewer

Surrounding area

Pocket 2 FPocket #1

0.243

Likely same site as P2Rank 1 2.4 Å 12 shared residues 86% of smaller site

Show in viewer

Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.411

Likely same site as FPocket 1 2.4 Å 15 shared residues 94% of smaller site

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.019

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.019

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #3

0.448

Show in viewer

Surrounding area

Pocket 2 FPocket #1

0.226

Likely same site as P2Rank 1 2.4 Å 15 shared residues 94% of smaller site

Show in viewer

Surrounding area

Pocket 3 FPocket #7

0.217 Unusual size

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_A0A0H3GKW4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04238	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.

48 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 2 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 46 similarity-based ZINC candidates

Best available ligand signal

FLC PDB via homolog 189.1 Da · LogP -5.25 · TPSA 140.6 Open detail RCSB PDB

J0J PDB via homolog Detail RCSB PDB

ZINC15722130 ZINC proposed compound · Tanimoto 0.745 Detail ZINC

ZINC255987061 ZINC proposed compound · Tanimoto 0.745 Detail ZINC

ZINC255987062 ZINC proposed compound · Tanimoto 0.745 Detail ZINC

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
FLC RCSB PDB	4BJ4	Q9HT86	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
J0J RCSB PDB	4BOL	Q9HT86	461.5 Da LogP -2.66 TPSA 251.2	1 viol.	✓ Clean	`C[C@H](C(=O)N[C@H](CCC(=O)N[C@@H](CCC[C@H](C(=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
ZINC15722130 ZINC	0.745	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@@H](CCCCN)C(=O)…`
ZINC255987061 ZINC	0.745	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@H](CCCCN)C(=O)N…`
ZINC255987062 ZINC	0.745	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@H](CCCCN)C(=O)N…`
ZINC255987063 ZINC	0.745	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@H](CCCCN)C(=O)N…`
ZINC255987064 ZINC	0.745	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@H](CCCCN)C(=O)N…`
ZINC13514803 ZINC	0.667	347.3 Da LogP -1.88 TPSA 196.1	1 viol.	✓ Clean	`C[C@H](NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=…`
ZINC13514809 ZINC	0.565	404.4 Da LogP -1.77 TPSA 222.1	1 viol.	✓ Clean	`NCCCC[C@H](NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O…`
ZINC2567650 ZINC	0.565	288.3 Da LogP -2.33 TPSA 164.6	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C…`
ZINC2242980 ZINC	0.558	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC2560662 ZINC	0.558	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@@H](N)C(=O)N[C@H](CCC(=O)O)C(=O)O`
ZINC15261541 ZINC	0.556	261.3 Da LogP -1.51 TPSA 155.7	✓ Ro5	✓ Clean	`NCCC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC1529737 ZINC	0.548	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC2384790 ZINC	0.548	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC2560745 ZINC	0.548	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC2560989 ZINC	0.548	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC1575564 ZINC	0.545	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCCC[C@H](NC(=O)[C@@H](C)N)C(=O)O`
ZINC1575565 ZINC	0.545	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCCC[C@@H](NC(=O)[C@@H](C)N)C(=O)O`
ZINC1575566 ZINC	0.545	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCCC[C@H](NC(=O)[C@H](C)N)C(=O)O`
ZINC1575567 ZINC	0.545	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCCC[C@@H](NC(=O)[C@H](C)N)C(=O)O`
ZINC2242694 ZINC	0.545	276.2 Da LogP -1.39 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC2504612 ZINC	0.545	217.2 Da LogP -1.83 TPSA 135.5	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC2547582 ZINC	0.545	276.2 Da LogP -1.39 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC2560934 ZINC	0.545	217.2 Da LogP -1.83 TPSA 135.5	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(N)=O)C(=O)O`
ZINC2560982 ZINC	0.545	217.2 Da LogP -1.83 TPSA 135.5	✓ Ro5	✓ Clean	`C[C@@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC3204007 ZINC	0.545	203.2 Da LogP -1.36 TPSA 118.4	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@@H](CCCN)C(=O)O`
ZINC4096970 ZINC	0.545	405.4 Da LogP -2.04 TPSA 233.4	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CCC(=O)N[C@@H](CCC(=O)O)…`
ZINC4523272 ZINC	0.545	217.2 Da LogP -1.83 TPSA 135.5	✓ Ro5	✓ Clean	`C[C@@H](N)C(=O)N[C@H](CCC(N)=O)C(=O)O`
ZINC4545890 ZINC	0.545	276.2 Da LogP -1.39 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC4545891 ZINC	0.545	276.2 Da LogP -1.39 TPSA 167.0	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC4726537 ZINC	0.538	453.4 Da LogP -2.47 TPSA 265.8	✓ Ro5	Alert	`[N-]=[N+]=CC(=O)CC[C@H](NC(=O)[C@H](CCC(=O)C=[N…`
ZINC2390999 ZINC	0.533	275.3 Da LogP -1.99 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC2522662 ZINC	0.533	217.3 Da LogP -0.97 TPSA 118.4	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)O`
ZINC2522687 ZINC	0.533	273.3 Da LogP -0.55 TPSA 121.5	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](C)N)C(=O)N[C@@H](C)C(=O…`
ZINC3014479 ZINC	0.533	217.3 Da LogP -0.97 TPSA 118.4	✓ Ro5	✓ Clean	`C[C@@H](N)C(=O)N[C@@H](CCCCN)C(=O)O`
ZINC3014482 ZINC	0.533	217.3 Da LogP -0.97 TPSA 118.4	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCCCN)C(=O)O`
ZINC3014483 ZINC	0.533	217.3 Da LogP -0.97 TPSA 118.4	✓ Ro5	✓ Clean	`C[C@@H](N)C(=O)N[C@H](CCCCN)C(=O)O`
ZINC15261332 ZINC	0.531	303.3 Da LogP -1.99 TPSA 191.6	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC5495961 ZINC	0.529	362.3 Da LogP -3.64 TPSA 208.1	1 viol.	✓ Clean	`C[C@H](N)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC…`
ZINC13507519 ZINC	0.523	234.2 Da LogP -2.26 TPSA 150.0	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CO)C(=O)O)C(=O)O`
ZINC2579085 ZINC	0.521	245.3 Da LogP -1.83 TPSA 154.3	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)O`
ZINC8577164 ZINC	0.521	245.3 Da LogP -1.83 TPSA 154.3	1 viol.	✓ Clean	`C[C@@H](N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)O`
ZINC15721478 ZINC	0.519	390.3 Da LogP -3.16 TPSA 225.2	1 viol.	✓ Clean	`C[C@H](NC(=O)[C@H](CCC(=O)O)NC(=O)CNC(=O)[C@@H]…`
ZINC3873037 ZINC	0.519	363.4 Da LogP -0.79 TPSA 158.8	1 viol.	✓ Clean	`CC(C)[C@@H](NC(=O)[C@H](CS)NC(=O)CCC[C@H](N)C(=…`
ZINC2504764 ZINC	0.511	232.2 Da LogP -0.84 TPSA 129.7	✓ Ro5	✓ Clean	`CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC2384788 ZINC	0.500	260.3 Da LogP -0.21 TPSA 129.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC4899571 ZINC	0.500	360.5 Da LogP -2.42 TPSA 199.6	1 viol.	✓ Clean	`NCCC[C@H](N)C(=O)N[C@@H](CCCN)C(=O)N[C@@H](CCCN…`

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.

Cross-references

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

Sequence

UniProt A0A0H3GKW4