Protein profile

KP13_32046

molybdopterin biosynthesis family protein

Genome: KpKP13

Gene: AHE45521.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GQC3

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Amino acids 411

Annotations 6

Features 37

PDB binders 9

Druggability 0.787

Overview

Basic information about this protein and its source genome.

Accession: KP13_32046
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE45521.1
Status: annotated
Amino acids: 411
Structure source: AlphaFold + ColabFold

2.10.1.1

GO:0032324 The chemical reactions and pathways resulting in the formation of the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands. GO:0006777 The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0046872 Binding to a metal ion. GO:0061599 Catalysis of the reaction adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 43.353
Human E-value: 9.64e-32
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 56.683
DEG E-value: 1.78e-165
Localization: Cytoplasmic
ColabFold pLDDT: 95.12

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 0.787

Structure A0A0H3GQC3

Pocket Pocket 12

P2Rank 0.697

Structure A0A0H3GQC3

Pocket Pocket 1

ColabFold model

FPocket 0.685 · Pocket 14

P2Rank 0.708 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 142 / 4744 genomes with a hit

Normalized 0.03

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)

2.10.1.1

Gene Ontology (GO)

GO:0032324 The chemical reactions and pathways resulting in the formation of the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
GO:0006777 The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0046872 Binding to a metal ion.
GO:0061599 Catalysis of the reaction adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.

Sequence Features

Domain/signature hits from InterPro and related databases.

37 records

Show feature table

Start	End	DB	Term	Name
1	15	Phobius	SIGNAL_PEPTIDE	Signal peptide region
1	2	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
181	318	SMART	SM00852	MoCF_biosynth_3a
181	318	InterPro	IPR001453	MoaB/Mog domain
9	168	Pfam	PF03453	MoeA N-terminal region (domain I and II)
9	168	InterPro	IPR005110	MoeA, N-terminal and linker domain
176	326	FunFam	G3DSA:3.40.980.10:FF:000004	Molybdopterin molybdenumtransferase
178	322	SUPERFAMILY	SSF53218	Molybdenum cofactor biosynthesis proteins
178	322	InterPro	IPR036425	MoaB/Mog-like domain superfamily
26	328	Gene3D	G3DSA:3.40.980.10	-
26	328	InterPro	IPR036425	MoaB/Mog-like domain superfamily
3	10	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
177	314	NCBIfam	TIGR00177	molybdenum cofactor biosynthesis domain
177	314	InterPro	IPR001453	MoaB/Mog domain
16	411	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
13	404	CDD	cd00887	MoeA
13	404	InterPro	IPR038987	Molybdopterin biosynthesis protein MoeA-like
27	175	Gene3D	G3DSA:3.90.105.10	Molybdopterin biosynthesis moea protein, domain 2
329	399	FunFam	G3DSA:2.40.340.10:FF:000003	Molybdopterin molybdenumtransferase
181	317	Pfam	PF00994	Probable molybdopterin binding domain
181	317	InterPro	IPR001453	MoaB/Mog domain
329	408	SUPERFAMILY	SSF63867	MoeA C-terminal domain-like
329	408	InterPro	IPR036688	MoeA, C-terminal, domain IV superfamily
329	399	Gene3D	G3DSA:2.40.340.10	-
329	399	InterPro	IPR036688	MoeA, C-terminal, domain IV superfamily
51	142	Gene3D	G3DSA:2.170.190.11	Molybdopterin biosynthesis moea protein, domain 3.
6	405	PANTHER	PTHR10192	MOLYBDOPTERIN BIOSYNTHESIS PROTEIN
6	405	InterPro	IPR038987	Molybdopterin biosynthesis protein MoeA-like
411	411	Coils	Coil	Coil
332	404	Pfam	PF03454	MoeA C-terminal region (domain IV)
332	404	InterPro	IPR005111	MoeA, C-terminal, domain IV
254	287	ProSitePatterns	PS01079	Molybdenum cofactor biosynthesis proteins signature 2.
254	287	InterPro	IPR008284	Molybdenum cofactor biosynthesis, conserved site
7	177	SUPERFAMILY	SSF63882	MoeA N-terminal region -like
7	177	InterPro	IPR036135	MoeA, N-terminal and linker domain superfamily
11	15	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
51	142	FunFam	G3DSA:2.170.190.11:FF:000001	Molybdopterin molybdenumtransferase

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

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_A0A0H3GQC3	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_32046	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
12				0.787

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	5.0	0.227
2	3.74	0.143
3	3.38	0.121
4	3.02	0.099

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				0.685

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	5.74	0.278
2	3.63	0.136
3	3.62	0.135
4	3.5	0.128

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.

59 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
3F7	6HSO	Q03555	268.2 Da LogP 0.55 TPSA 74.8	✓ Ro5	✓ Clean	`c1cc(ccc1N2C(=O)C=CC2=O)N3C(=O)C=CC3=O`
3F8	6HSN	Q03555	308.3 Da LogP -1.13 TPSA 93.2	✓ Ro5	✓ Clean	`C1=CC(=O)N(C1=O)CCOCCOCCN2C(=O)C=CC2=O`
D8Z	6FGD	Q03555	298.4 Da LogP 2.84 TPSA 46.2	✓ Ro5	✓ Clean	`C[C@@H]1CC[C@H]2[C@H]([C@H](O[C@H]3[C@@]24[C@H]…`
D95	6FGC	Q03555	384.4 Da LogP 2.60 TPSA 100.5	✓ Ro5	✓ Clean	`C[C@@H]1CC[C@H]2[C@H]([C@@H](O[C@H]3[C@@]24[C@H…`
MO	5ERU	Q03555	95.9 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Mo]`
MOO	5ERU	Q03555	159.9 Da LogP -2.62 TPSA 80.3	✓ Ro5	✓ Clean	`[O-][Mo](=O)(=O)[O-]`
NWS	6Q32	Q39054	868.5 Da LogP -2.05 TPSA 384.2	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
W	5ERV	Q03555	183.8 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[W+6]`
WO4	5ERV	Q03555	247.8 Da LogP -2.62 TPSA 80.3	✓ Ro5	✓ Clean	`[O-][W](=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
ZINC145341967	1.000	440.4 Da LogP -1.08 TPSA 120.9	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC156949	1.000	268.2 Da LogP 0.55 TPSA 74.8	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1c1ccc(N2C(=O)C=CC2=O)cc1`
ZINC1857792026	1.000	484.5 Da LogP -1.06 TPSA 130.1	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2387138	1.000	352.3 Da LogP -1.11 TPSA 102.4	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2572930	1.000	308.3 Da LogP -1.13 TPSA 93.2	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCN1C(=O)C=CC1=O`
ZINC5372881	1.000	396.4 Da LogP -1.10 TPSA 111.7	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC64608163	1.000	384.4 Da LogP 2.60 TPSA 100.5	✓ Ro5	✓ Clean	`C[C@@H]1[C@H](OC(=O)CCC(=O)O)O[C@H]2O[C@@]3(C)C…`
ZINC77273545	0.950	264.2 Da LogP -1.15 TPSA 84.0	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCN1C(=O)C=CC1=O`
ZINC1591996	0.833	344.3 Da LogP 2.21 TPSA 74.8	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1c1ccc(-c2ccc(N3C(=O)C=CC3=O)cc2)c…`
ZINC113221622	0.800	229.2 Da LogP -1.06 TPSA 76.1	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCO`
ZINC1857791904	0.800	449.5 Da LogP -0.98 TPSA 122.2	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1857792820	0.800	316.4 Da LogP -1.06 TPSA 100.3	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC1857792836	0.800	360.4 Da LogP -1.05 TPSA 109.6	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC211225534	0.800	361.4 Da LogP -1.01 TPSA 103.8	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCOCCO`
ZINC224746938	0.800	272.3 Da LogP -1.08 TPSA 91.1	✓ Ro5	✓ Clean	`NCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2332239859	0.800	404.5 Da LogP -1.03 TPSA 118.8	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC44831087	0.800	228.2 Da LogP -1.10 TPSA 81.9	✓ Ro5	✓ Clean	`NCCOCCOCCN1C(=O)C=CC1=O`
ZINC585665970	0.800	317.3 Da LogP -1.03 TPSA 94.5	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCO`
ZINC96299624	0.800	273.3 Da LogP -1.05 TPSA 85.3	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCO`
ZINC106362085	0.758	455.5 Da LogP 2.11 TPSA 129.6	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)CCC(=O)O[C@@H]1O[C@@H]2O[C@]3(C)C…`
ZINC14362	0.750	299.1 Da LogP 1.72 TPSA 37.4	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1c1ccc(I)cc1`
ZINC96640	0.750	207.6 Da LogP 1.77 TPSA 37.4	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1c1ccc(Cl)cc1`
ZINC97319	0.750	252.1 Da LogP 1.88 TPSA 37.4	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1c1ccc(Br)cc1`
ZINC106362035	0.734	481.5 Da LogP 2.59 TPSA 120.8	✓ Ro5	✓ Clean	`C[C@@H]1CC[C@H]2[C@@H](C)[C@H](OC(=O)CCC(=O)N3C…`
ZINC106362063	0.734	471.5 Da LogP 1.08 TPSA 149.8	✓ Ro5	✓ Clean	`C[C@@H]1CC[C@H]2[C@@H](C)[C@H](OC(=O)CCC(=O)N[C…`
ZINC106362113	0.734	483.6 Da LogP 2.74 TPSA 129.6	✓ Ro5	✓ Clean	`CC(C)[C@@H](NC(=O)CCC(=O)O[C@@H]1O[C@@H]2O[C@]3…`
ZINC106362067	0.723	485.5 Da LogP 1.47 TPSA 149.8	✓ Ro5	✓ Clean	`C[C@@H]1CC[C@H]2[C@@H](C)[C@H](OC(=O)CCC(=O)N[C…`
ZINC229932341	0.723	485.5 Da LogP 1.47 TPSA 149.9	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H](NC(=O)CCC(=O)O[C@@H]1O[C@@H]2O[…`
ZINC229932354	0.723	485.5 Da LogP 1.47 TPSA 149.9	✓ Ro5	✓ Clean	`C[C@H](O)[C@H](NC(=O)CCC(=O)O[C@@H]1O[C@@H]2O[C…`
ZINC1046144	0.714	358.4 Da LogP 2.14 TPSA 74.8	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1c1ccc(Cc2ccc(N3C(=O)C=CC3=O)cc2)c…`
ZINC205372234	0.714	311.3 Da LogP -0.39 TPSA 74.3	✓ Ro5	✓ Clean	`C#CCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2060424636	0.714	355.4 Da LogP -0.37 TPSA 83.5	✓ Ro5	✓ Clean	`C#CCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2069469067	0.714	359.4 Da LogP -0.32 TPSA 74.3	✓ Ro5	✓ Clean	`C[N+](C)(C)CCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2069557053	0.714	403.5 Da LogP -0.30 TPSA 83.5	✓ Ro5	✓ Clean	`C[N+](C)(C)CCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC230833776	0.714	287.3 Da LogP -0.95 TPSA 102.4	✓ Ro5	✓ Clean	`O=C(O)COCCOCCOCCN1C(=O)C=CC1=O`
ZINC230833805	0.714	331.3 Da LogP -0.94 TPSA 111.6	✓ Ro5	✓ Clean	`O=C(O)COCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC230833838	0.714	375.4 Da LogP -0.92 TPSA 120.8	✓ Ro5	✓ Clean	`O=C(O)COCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC230833875	0.714	419.4 Da LogP -0.90 TPSA 130.1	✓ Ro5	✓ Clean	`O=C(O)COCCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC38622096	0.714	372.3 Da LogP 2.96 TPSA 99.5	✓ Ro5	Alert	`O=C1C=CC(=O)N1c1ccc(/N=N/c2ccc(N3C(=O)C=CC3=O)c…`
ZINC38919019	0.714	243.2 Da LogP -0.97 TPSA 93.1	✓ Ro5	✓ Clean	`O=C(O)COCCOCCN1C(=O)C=CC1=O`
ZINC71257140	0.714	345.3 Da LogP -0.55 TPSA 111.6	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC79016605	0.714	433.5 Da LogP -0.51 TPSA 130.1	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC823759	0.714	376.4 Da LogP 2.70 TPSA 74.8	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1c1ccc(Sc2ccc(N3C(=O)C=CC3=O)cc2)c…`
ZINC826893	0.714	360.3 Da LogP 2.34 TPSA 84.0	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1c1ccc(Oc2ccc(N3C(=O)C=CC3=O)cc2)c…`
ZINC842474	0.714	452.4 Da LogP 4.13 TPSA 93.2	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1c1ccc(Oc2ccc(Oc3ccc(N4C(=O)C=CC4=…`
ZINC96300340	0.714	257.2 Da LogP -0.58 TPSA 93.1	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCN1C(=O)C=CC1=O`
ZINC96300342	0.714	301.3 Da LogP -0.56 TPSA 102.4	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC96503541	0.714	389.4 Da LogP -0.53 TPSA 120.8	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC106362148	0.712	497.6 Da LogP 3.13 TPSA 129.6	✓ Ro5	✓ Clean	`CC(C)C[C@@H](NC(=O)CCC(=O)O[C@@H]1O[C@@H]2O[C@]…`
ZINC229932392	0.712	497.5 Da LogP 1.56 TPSA 141.1	✓ Ro5	✓ Clean	`C[C@@H]1CC[C@H]2[C@@H](C)[C@H](OC(=O)CCC(=O)N3C…`

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.