KpKP13 Protein target profile

Molybdopterin adenylyltransferase

Accession: KP13_01986

Gene: mog AHE46424.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GMZ7

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Length 195

Pocket druggability (P2Rank · AlphaFold DB model) 0.821

Direct ligand evidence 0 60 total records

Functional annotation 1 EC 3 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.

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.82. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 10 structural and 0 bioactivity records.

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: Hit
Human identity (%): 40.0 Lower values reduce human off-target concern.
Human E-value: 5.91e-18
Gut microbiome similarity: 4.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 91.146 Higher values support similarity to known essential genes.
DEG E-value: 6.429999999999999e-131 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.96 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) 0.821

Structure A0A0H3GMZ7

Pocket Pocket 1

Druggability (FPocket) 0.296

Structure A0A0H3GMZ7

Pocket Pocket 1

ColabFold model

P2Rank 0.786 · Pocket 1

FPocket 0.672 · Pocket 2

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 218 / 4744 genomes with a hit

Prevalence 4.6%

Sequence

Primary amino-acid sequence viewer.

MNTLRIGLVSISDRASSGVYQDKGIPALEEWLARALTTPFELQTRLIPDEQATIEQTLCELVDEMGCHLVLTTGGTGPARRDVTPDATLAIADREMPGFGEQMRQVSLHFVPTAILSRQVGVIRKQALILNLPGQPKAIQETLEGVKDADGNVLVHGIFASVPYCVQLLEGPYVETDGRVVEAFRPKSARRETLS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 3 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.7.7.75

Gene Ontology (GO)

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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0061598 Catalysis of the reaction ATP + molybdopterin = diphosphate + adenylyl-molybdopterin.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

16 records

Show feature table

Start	End	DB	Term	Name
4	146	NCBIfam	TIGR00177	molybdenum cofactor biosynthesis domain
4	146	InterPro	IPR001453	MoaB/Mog domain
8	147	Pfam	PF00994	Probable molybdopterin binding domain
8	147	InterPro	IPR001453	MoaB/Mog domain
4	156	CDD	cd00886	MogA_MoaB
4	156	InterPro	IPR001453	MoaB/Mog domain
3	188	SUPERFAMILY	SSF53218	Molybdenum cofactor biosynthesis proteins
3	188	InterPro	IPR036425	MoaB/Mog-like domain superfamily
7	153	SMART	SM00852	MoCF_biosynth_3a
7	153	InterPro	IPR001453	MoaB/Mog domain
69	82	ProSitePatterns	PS01078	Molybdenum cofactor biosynthesis proteins signature 1.
69	82	InterPro	IPR008284	Molybdenum cofactor biosynthesis, conserved site
1	195	Gene3D	G3DSA:3.40.980.10	-
1	195	InterPro	IPR036425	MoaB/Mog-like domain superfamily
1	176	PANTHER	PTHR43764	MOLYBDENUM COFACTOR BIOSYNTHESIS
1	194	FunFam	G3DSA:3.40.980.10:FF:000005	Molybdopterin biosynthesis mog protein

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 · P2Rank

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

Pocket 1 P2Rank #1

0.821

Likely same site as FPocket 1 6.5 Å 14 shared residues 78% of smaller site

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.296 Unusual size

Likely same site as P2Rank 1 6.5 Å 14 shared residues 78% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #6

0.267

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_A0A0H3GMZ7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01986	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.

60 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 10 records from similar proteins

Structural ligands 10 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3F7 PDB via homolog 268.2 Da · LogP 0.55 · TPSA 74.8 Open detail RCSB PDB

3F8 PDB via homolog Detail RCSB PDB

B3P PDB via homolog Detail RCSB PDB

D8Z PDB via homolog Detail RCSB PDB

D95 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
3F7 RCSB PDB	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 RCSB PDB	6HSN	Q03555	308.3 Da LogP -1.13 TPSA 93.2	✓ Ro5	✓ Clean	`C1=CC(=O)N(C1=O)CCOCCOCCN2C(=O)C=CC2=O`
B3P RCSB PDB	3RFQ	B2HEA7	282.3 Da LogP -4.01 TPSA 145.4	1 viol.	✓ Clean	`C(CNC(CO)(CO)CO)CNC(CO)(CO)CO`
D8Z RCSB PDB	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 RCSB PDB	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 RCSB PDB	5ERU	Q03555	95.9 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Mo]`
MOO RCSB PDB	5ERU	Q03555	159.9 Da LogP -2.62 TPSA 80.3	✓ Ro5	✓ Clean	`[O-][Mo](=O)(=O)[O-]`
NWS RCSB PDB	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 RCSB PDB	5ERV	Q03555	183.8 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[W+6]`
WO4 RCSB PDB	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 ZINC	1.000	440.4 Da LogP -1.08 TPSA 120.9	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC156949 ZINC	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 ZINC	1.000	484.5 Da LogP -1.06 TPSA 130.1	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2387138 ZINC	1.000	352.3 Da LogP -1.11 TPSA 102.4	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2572930 ZINC	1.000	308.3 Da LogP -1.13 TPSA 93.2	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCN1C(=O)C=CC1=O`
ZINC4521259 ZINC	1.000	282.3 Da LogP -4.01 TPSA 145.4	1 viol.	✓ Clean	`OCC(CO)(CO)NCCCNC(CO)(CO)CO`
ZINC5372881 ZINC	1.000	396.4 Da LogP -1.10 TPSA 111.7	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC64608163 ZINC	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 ZINC	0.950	264.2 Da LogP -1.15 TPSA 84.0	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCN1C(=O)C=CC1=O`
ZINC1591996 ZINC	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 ZINC	0.800	229.2 Da LogP -1.06 TPSA 76.1	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCO`
ZINC1857791904 ZINC	0.800	449.5 Da LogP -0.98 TPSA 122.2	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1857792820 ZINC	0.800	316.4 Da LogP -1.06 TPSA 100.3	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC1857792836 ZINC	0.800	360.4 Da LogP -1.05 TPSA 109.6	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC211225534 ZINC	0.800	361.4 Da LogP -1.01 TPSA 103.8	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCOCCO`
ZINC224746938 ZINC	0.800	272.3 Da LogP -1.08 TPSA 91.1	✓ Ro5	✓ Clean	`NCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2332239859 ZINC	0.800	404.5 Da LogP -1.03 TPSA 118.8	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC44831087 ZINC	0.800	228.2 Da LogP -1.10 TPSA 81.9	✓ Ro5	✓ Clean	`NCCOCCOCCN1C(=O)C=CC1=O`
ZINC585665970 ZINC	0.800	317.3 Da LogP -1.03 TPSA 94.5	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCO`
ZINC96299624 ZINC	0.800	273.3 Da LogP -1.05 TPSA 85.3	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCO`
ZINC106362085 ZINC	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 ZINC	0.750	299.1 Da LogP 1.72 TPSA 37.4	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1c1ccc(I)cc1`
ZINC96640 ZINC	0.750	207.6 Da LogP 1.77 TPSA 37.4	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1c1ccc(Cl)cc1`
ZINC97319 ZINC	0.750	252.1 Da LogP 1.88 TPSA 37.4	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1c1ccc(Br)cc1`
ZINC106362035 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	0.714	311.3 Da LogP -0.39 TPSA 74.3	✓ Ro5	✓ Clean	`C#CCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2060424636 ZINC	0.714	355.4 Da LogP -0.37 TPSA 83.5	✓ Ro5	✓ Clean	`C#CCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2069469067 ZINC	0.714	359.4 Da LogP -0.32 TPSA 74.3	✓ Ro5	✓ Clean	`C[N+](C)(C)CCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2069557053 ZINC	0.714	403.5 Da LogP -0.30 TPSA 83.5	✓ Ro5	✓ Clean	`C[N+](C)(C)CCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC230833776 ZINC	0.714	287.3 Da LogP -0.95 TPSA 102.4	✓ Ro5	✓ Clean	`O=C(O)COCCOCCOCCN1C(=O)C=CC1=O`
ZINC230833805 ZINC	0.714	331.3 Da LogP -0.94 TPSA 111.6	✓ Ro5	✓ Clean	`O=C(O)COCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC230833838 ZINC	0.714	375.4 Da LogP -0.92 TPSA 120.8	✓ Ro5	✓ Clean	`O=C(O)COCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC230833875 ZINC	0.714	419.4 Da LogP -0.90 TPSA 130.1	✓ Ro5	✓ Clean	`O=C(O)COCCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC38622096 ZINC	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 ZINC	0.714	243.2 Da LogP -0.97 TPSA 93.1	✓ Ro5	✓ Clean	`O=C(O)COCCOCCN1C(=O)C=CC1=O`
ZINC71257140 ZINC	0.714	345.3 Da LogP -0.55 TPSA 111.6	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC79016605 ZINC	0.714	433.5 Da LogP -0.51 TPSA 130.1	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC823759 ZINC	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 ZINC	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 ZINC	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 ZINC	0.714	257.2 Da LogP -0.58 TPSA 93.1	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCN1C(=O)C=CC1=O`
ZINC96300342 ZINC	0.714	301.3 Da LogP -0.56 TPSA 102.4	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC96503541 ZINC	0.714	389.4 Da LogP -0.53 TPSA 120.8	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC229932392 ZINC	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.

Cross-references

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

Sequence

UniProt A0A0H3GMZ7