Protein target profile

KP13_00750

50S ribosomal protein L4

Genome: KpKP13 Gene: AHE42367.1 rplD 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GU26

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Length 201

Pocket druggability 0.261

Direct ligand evidence 0 57 total records

Functional annotation 0 EC 5 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing 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: Hit
Human identity (%): 56.14 Lower values reduce human off-target concern.
Human E-value: 3.53e-14
Gut microbiome similarity: 5.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 99.005 Higher values support similarity to known essential genes.
DEG E-value: 8.699999999999999e-147 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 95.43 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 0.261

Structure A0A0H3GU26

Pocket Pocket 2

P2Rank 0.007

Structure A0A0H3GU26

Pocket Pocket 1

ColabFold model

FPocket 0.292 · Pocket 4

P2Rank 0.014 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 240 / 4744 genomes with a hit

Prevalence 5.1%

Cross-references

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

Sequence

UniProt A0A0H3GU26

Sequence

Primary amino-acid sequence viewer.

MELVLKDAQSALTVSETTFGRDFNEALVHQVVVAYAAGARQGTRAQKTRAEITGSGKKPWRQKGTGRARSGSIKSPIWRSGGVTFAARPQDHSQKVNKKMYRGALKSILSELVRQDRLIVVEKFSVEAPKTKLLAQKLKDMALEDVLIITGELDENLFLAARNLHKVDVRDANGIDPVSLIAFDKVVMTADAVKQVEEMLA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.
GO:0005840 An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins.
GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
GO:1990904 A macromolecular complex that contains both RNA and protein molecules.
GO:0019843 Binding to a ribosomal RNA.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

13 records

Show feature table

Start	End	DB	Term	Name
1	201	Gene3D	G3DSA:3.40.1370.10	-
1	201	InterPro	IPR023574	Ribosomal protein L4 domain superfamily
10	200	PANTHER	PTHR10746	50S RIBOSOMAL PROTEIN L4
10	200	InterPro	IPR013005	50S ribosomal protein uL4
10	200	SUPERFAMILY	SSF52166	Ribosomal protein L4
10	200	InterPro	IPR023574	Ribosomal protein L4 domain superfamily
6	201	Hamap	MF_01328_B	50S ribosomal protein L4 [rplD].
6	201	InterPro	IPR013005	50S ribosomal protein uL4
1	201	FunFam	G3DSA:3.40.1370.10:FF:000001	50S ribosomal protein L4
13	198	NCBIfam	TIGR03953	50S ribosomal protein L4
13	198	InterPro	IPR013005	50S ribosomal protein uL4
13	198	Pfam	PF00573	Ribosomal protein L4/L1 family
13	198	InterPro	IPR002136	Ribosomal protein L4/L1e

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

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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 #2

0.261

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.007

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_A0A0H3GU26	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00750	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.

57 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

5MU PDB via homolog 338.2 Da · LogP -2.43 · TPSA 171.3 Open detail RCSB PDB

FSD PDB via homolog Detail RCSB PDB

LUJ PDB via homolog Detail RCSB PDB

O PDB via homolog Detail RCSB PDB

OHX 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
5MU RCSB PDB	6O97	Q5SHN9	338.2 Da LogP -2.43 TPSA 171.3	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
FSD RCSB PDB	6CZR	Q5SHN9	618.7 Da LogP -0.38 TPSA 210.7	3 viol.	✓ Clean	`C[C@@H]1[C@H](CC[C@@H](O1)N2C=CC(=NC2=O)NC(=O)c…`
LUJ RCSB PDB	6O97	Q5SHN9	641.7 Da LogP -6.81 TPSA 327.1	3 viol.	✓ Clean	`CCC[C@@H]1[C@H](O[C@@H]([C@@H]([C@H]1O)N)O[C@@H…`
O RCSB PDB	5LI0	Q2FW07	18.0 Da LogP -0.82 TPSA 31.5	✓ Ro5	✓ Clean	`O`
OHX RCSB PDB	4V8E	Q5SHN9	286.4 Da LogP -3.55 TPSA 156.1	1 viol.	✓ Clean	`N[Os](N)(N)(N)(N)N`
PSU RCSB PDB	6O97	Q5SHN9	324.2 Da LogP -2.67 TPSA 182.2	1 viol.	✓ Clean	`C1=C(C(=O)NC(=O)N1)[C@H]2[C@@H]([C@@H]([C@H](O2…`
SPD RCSB PDB	4WFA	Q2FW07	145.2 Da LogP -0.34 TPSA 64.1	✓ Ro5	✓ Clean	`C(CCNCCCN)CN`

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
ZINC13515793 ZINC	1.000	338.2 Da LogP -2.43 TPSA 171.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H]2…`
ZINC27564039 ZINC	0.933	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCNCCCN`
ZINC13377742 ZINC	0.929	230.4 Da LogP 0.42 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCCNCCCCN`
ZINC1532734 ZINC	0.929	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCNCCCCNCCCN`
ZINC1598087 ZINC	0.867	215.4 Da LogP 1.61 TPSA 64.1	✓ Ro5	✓ Clean	`NCCCCCCNCCCCCCN`
ZINC13518650 ZINC	0.837	418.2 Da LogP -2.31 TPSA 217.8	1 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[C…`
ZINC65748564 ZINC	0.813	484.1 Da LogP -2.43 TPSA 275.2	2 viol.	✓ Clean	`O=c1[nH]cc([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=…`
ZINC65748567 ZINC	0.813	484.1 Da LogP -2.43 TPSA 275.2	2 viol.	✓ Clean	`O=c1[nH]cc([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=…`
ZINC77312680 ZINC	0.813	484.1 Da LogP -2.43 TPSA 275.2	2 viol.	✓ Clean	`O=c1[nH]cc([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=…`
ZINC13519607 ZINC	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)OP…`
ZINC31298140 ZINC	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC81168754 ZINC	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC81168756 ZINC	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC13518175 ZINC	0.755	450.1 Da LogP -2.13 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC13523519 ZINC	0.720	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC1532628 ZINC	0.720	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC1678872 ZINC	0.720	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=O…`
ZINC2047010 ZINC	0.720	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3870253 ZINC	0.720	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3870254 ZINC	0.720	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O)…`
ZINC6523446 ZINC	0.720	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=…`
ZINC100052153 ZINC	0.712	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC100223147 ZINC	0.712	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@@H](O[C@@H]2[C@@H](O[C@@H]3O[C@H](…`
ZINC103649633 ZINC	0.712	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC242575106 ZINC	0.712	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC242575107 ZINC	0.712	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC242575108 ZINC	0.712	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC242575109 ZINC	0.712	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC43664294 ZINC	0.712	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC43664297 ZINC	0.712	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC43664300 ZINC	0.712	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC43664303 ZINC	0.712	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC53255716 ZINC	0.712	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC56874669 ZINC	0.712	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
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`
ZINC205346095 ZINC	0.698	369.2 Da LogP -2.83 TPSA 214.4	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC2046807 ZINC	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O)[n…`
ZINC2125635 ZINC	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=O)[…`
ZINC21999938 ZINC	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)[n…`
ZINC2583634 ZINC	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)[n…`
ZINC4028557 ZINC	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)[nH…`
ZINC4557135 ZINC	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)[n…`
ZINC4557136 ZINC	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)[…`
ZINC4557137 ZINC	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=O)…`
ZINC5765081 ZINC	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)[…`
ZINC13519179 ZINC	0.667	244.2 Da LogP -2.78 TPSA 135.6	✓ Ro5	✓ Clean	`O=c1[nH]cc([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c…`
ZINC4602229 ZINC	0.667	288.3 Da LogP -3.18 TPSA 145.0	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H](O)[C@H]…`
ZINC5022258 ZINC	0.667	244.2 Da LogP -2.78 TPSA 135.6	✓ Ro5	✓ Clean	`O=c1[nH]cc([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c…`
ZINC5022260 ZINC	0.667	244.2 Da LogP -2.78 TPSA 135.6	✓ Ro5	✓ Clean	`O=c1[nH]cc([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)…`

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.

KP13_00750

Target candidate with partial support; inspect missing evidence before prioritizing.

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Sequence

Functional annotations

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence