9z4x

MENIN IN COMPLEX WITH JNJ-75276617 (Bleximenib)

Method: X-RAY DIFFRACTION D_max: 178.2 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Menin

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 2–610	Not recorded	BME BETA-MERCAPTOETHANOL × 1 9N6 N-ethyl-5-fluoro-2-{[5-(2-{(3R)-6-[(2-methoxyethyl)(methyl)amino]-2-methylhexan-3-yl}-2,6-diazaspiro[3.4]octan-6-yl)-1,2,4-triazin-6-yl]oxy}-N-(propan-2-yl)benzamide × 1 NA SODIUM ION × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；293 K；100 mM Tris pH 6.75 , 5 M NaCl , 0.2 M MgCl2	Resolution 2.95 Å R-free 0.297
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 2–610	Not recorded	BME BETA-MERCAPTOETHANOL × 1 9N6 N-ethyl-5-fluoro-2-{[5-(2-{(3R)-6-[(2-methoxyethyl)(methyl)amino]-2-methylhexan-3-yl}-2,6-diazaspiro[3.4]octan-6-yl)-1,2,4-triazin-6-yl]oxy}-N-(propan-2-yl)benzamide × 1 NA SODIUM ION × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；293 K；100 mM Tris pH 6.75 , 5 M NaCl , 0.2 M MgCl2	Resolution 2.95 Å R-free 0.297
3	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain C； UniProt 2–610	Not recorded	9N6 N-ethyl-5-fluoro-2-{[5-(2-{(3R)-6-[(2-methoxyethyl)(methyl)amino]-2-methylhexan-3-yl}-2,6-diazaspiro[3.4]octan-6-yl)-1,2,4-triazin-6-yl]oxy}-N-(propan-2-yl)benzamide × 1 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；293 K；100 mM Tris pH 6.75 , 5 M NaCl , 0.2 M MgCl2	Resolution 2.95 Å R-free 0.297
4	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain D； UniProt 2–610	Not recorded	9N6 N-ethyl-5-fluoro-2-{[5-(2-{(3R)-6-[(2-methoxyethyl)(methyl)amino]-2-methylhexan-3-yl}-2,6-diazaspiro[3.4]octan-6-yl)-1,2,4-triazin-6-yl]oxy}-N-(propan-2-yl)benzamide × 1 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；293 K；100 mM Tris pH 6.75 , 5 M NaCl , 0.2 M MgCl2	Resolution 2.95 Å R-free 0.297

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 9Z4X	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3U84 Crystal Structure of Human Menin Deposited 2011-10-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–459（458 aa） Chain A 520–610（91 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；1.4 M sodium acetate, pH 6.5, vapor diffusion, sitting drop, temperature 277K	Resolution 2.50 Å R-free 0.235
3U84 Crystal Structure of Human Menin Deposited 2011-10-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–459（458 aa） Chain B 520–610（91 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；1.4 M sodium acetate, pH 6.5, vapor diffusion, sitting drop, temperature 277K	Resolution 2.50 Å R-free 0.235
3U84 Crystal Structure of Human Menin Deposited 2011-10-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–459（458 aa） Chain A 520–610（91 aa） Chain B 2–459（458 aa） Chain B 520–610（91 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；1.4 M sodium acetate, pH 6.5, vapor diffusion, sitting drop, temperature 277K	Resolution 2.50 Å R-free 0.235
3U85 Crystal structure of human menin in complex with MLL1 Deposited 2011-10-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–459（458 aa） Chain A 520–610（91 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；2.3 M NaCl, pH 7.0, vapor diffusion, sitting drop, temperature 277K	Resolution 3.00 Å R-free 0.258
3U85 Crystal structure of human menin in complex with MLL1 Deposited 2011-10-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 2–459（458 aa） Chain A 520–610（91 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；2.3 M NaCl, pH 7.0, vapor diffusion, sitting drop, temperature 277K	Resolution 3.00 Å R-free 0.258
3U86 Crystal structure of human menin in complex with JunD Deposited 2011-10-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–459（458 aa） Chain A 520–610（91 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；2.3 M NaCl, pH 7.0, vapor diffusion, sitting drop, temperature 277K	Resolution 2.84 Å R-free 0.245
3U88 Crystal structure of human menin in complex with MLL1 and LEDGF Deposited 2011-10-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 2–459（458 aa） Chain A 520–610（91 aa）	Not recorded	CHD CHOLIC ACID × 1 GGB L-CANAVANINE × 4 0BR (4beta,8alpha,9R)-6'-methoxy-10,11-dihydrocinchonan-9-ol × 1 GLV GLYOXYLIC ACID × 4 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；277 K；1.6 M ammonium sulfate, pH 7.0, vapor diffusion, hanging drop, temperature 277K	Resolution 3.00 Å R-free 0.233
3U88 Crystal structure of human menin in complex with MLL1 and LEDGF Deposited 2011-10-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 2–459（458 aa） Chain B 520–610（91 aa）	Not recorded	CHD CHOLIC ACID × 1 GGB L-CANAVANINE × 1 0BR (4beta,8alpha,9R)-6'-methoxy-10,11-dihydrocinchonan-9-ol × 1 GLV GLYOXYLIC ACID × 2 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；277 K；1.6 M ammonium sulfate, pH 7.0, vapor diffusion, hanging drop, temperature 277K	Resolution 3.00 Å R-free 0.233
4GPQ Structural insights into inhibition of the bivalent menin-MLL interaction by small molecules in leukemia Deposited 2012-08-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–593（593 aa）	Mutation：A541t	PEG DI(HYDROXYETHYL)ETHER × 2 PG4 TETRAETHYLENE GLYCOL × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, VAPOR DIFFUSION, SITTING DROP	Resolution 1.46 Å R-free 0.176
4GQ3 Human menin with bound inhibitor MI-2 Deposited 2012-08-22	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–593（593 aa）	Mutation：A541t	0RO 4-[4-(5,5-dimethyl-4,5-dihydro-1,3-thiazol-2-yl)piperazin-1-yl]-6-propylthieno[2,3-d]pyrimidine × 1 PEG DI(HYDROXYETHYL)ETHER × 1 UNX UNKNOWN LIGAND × 5 SO4 SULFATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；283 K；0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, 200 mM 0RO, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 1.56 Å R-free 0.214
4GQ4 Human menin with bound inhibitor MI-2-2 Deposited 2012-08-22	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–593（593 aa）	Mutation：a541t	0RT 4-[4-(5,5-dimethyl-4,5-dihydro-1,3-thiazol-2-yl)piperazin-1-yl]-6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidine × 1 UNX UNKNOWN LIGAND × 5 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 SO4 SULFATE ION × 4 PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 2 DMS DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), NBm1 peptide, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, 200 mM 0RT, VAPOR DIFFUSION, SITTING DROP	Resolution 1.27 Å R-free 0.182
4GQ6 Human menin in complex with MLL peptide Deposited 2012-08-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–593（593 aa）	Mutation：a541t	SO4 SULFATE ION × 3 1PE PENTAETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；283 K；0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), NBm1 peptide, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, 1:1 molar ratio with MBM1 peptide, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 1.55 Å R-free 0.189
4I80 Crystal structure of human menin in complex with a high-affinity macrocyclic peptidomimetics Deposited 2012-12-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 2–459（458 aa） Chain A 520–610（91 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；277 K；2.3 M NaCl, pH 7.0, vapor diffusion, sitting drop, temperature 277K	Resolution 3.10 Å R-free 0.245
4OG3 Human menin with bound inhibitor MIV-3R Deposited 2014-01-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–593（593 aa）	Not recorded	SO4 SULFATE ION × 1 2S6 4-(3-{4-[(R)-cyclopentyl(hydroxy)phenylmethyl]piperidin-1-yl}propoxy)benzonitrile × 1 PG4 TETRAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 2 DMS DIMETHYL SULFOXIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 2.01 Å R-free 0.208
4OG4 Human menin with bound inhibitor MIV-3S Deposited 2014-01-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–593（593 aa）	Not recorded	SO4 SULFATE ION × 1 2VK 4-(3-{4-[(S)-cyclopentyl(hydroxy)phenylmethyl]piperidin-1-yl}propoxy)benzonitrile × 1 PG4 TETRAETHYLENE GLYCOL × 1 PGE TRIETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 2 DMS DIMETHYL SULFOXIDE × 4 TBF TERT-BUTYL FORMATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 1.45 Å R-free 0.189
4OG5 Human menin with bound inhibitor MIV-5 Deposited 2014-01-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–593（593 aa）	Not recorded	2S7 4-(3-{4-[(S)-cyclopentyl(hydroxy)pyridin-2-ylmethyl]piperidin-1-yl}propoxy)benzonitrile × 1 SO4 SULFATE ION × 2 PG4 TETRAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1 DMS DIMETHYL SULFOXIDE × 3 TBF TERT-BUTYL FORMATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 1.63 Å R-free 0.194
4OG6 Human menin with bound inhibitor MIV-4 Deposited 2014-01-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–593（593 aa）	Not recorded	SO4 SULFATE ION × 1 2S9 4-(3-{4-[(R)-cyclopentyl(3-fluorophenyl)hydroxymethyl]piperidin-1-yl}propoxy)benzonitrile × 1 PG4 TETRAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 3 DMS DIMETHYL SULFOXIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 1.49 Å R-free 0.188
4OG7 Human menin with bound inhibitor MIV-7 Deposited 2014-01-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–593（593 aa）	Not recorded	SO4 SULFATE ION × 1 2SE 4-(3-{4-[(S)-cyclopentyl(hydroxy)pyridin-2-ylmethyl]piperidin-1-yl}propoxy)benzenesulfonamide × 1 PGE TRIETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 2 DMS DIMETHYL SULFOXIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 2.08 Å R-free 0.222
4OG8 Human menin with bound inhibitor MIV-6R Deposited 2014-01-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–593（593 aa）	Not recorded	TBF TERT-BUTYL FORMATE × 2 2SF 4-(3-{4-[(R)-amino(cyclopentyl)phenylmethyl]piperidin-1-yl}propoxy)benzonitrile × 1 PG4 TETRAETHYLENE GLYCOL × 1 SO4 SULFATE ION × 3 DMS DIMETHYL SULFOXIDE × 3 PGA 2-PHOSPHOGLYCOLIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 1.53 Å R-free 0.176
4X5Y Menin in complex with MI-503 Deposited 2014-12-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Fragment：unp residues 1-459; unp residues 537-593 Chain A 537–593（57 aa） Fragment：unp residues 1-459; unp residues 537-593	Mutation：A541T Mutation：A541T	3XW 4-methyl-1-(1H-pyrazol-4-ylmethyl)-5-[(4-{[6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidin-4-yl]amino}piperidin-1-yl)methyl]-1H-indole-2-carbonitrile × 1 DMS DIMETHYL SULFOXIDE × 3 PG4 TETRAETHYLENE GLYCOL × 1 SO4 SULFATE ION × 3 EDO 1,2-ETHANEDIOL × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen	Resolution 1.59 Å R-free 0.205
4X5Z menin in complex with MI-136 Deposited 2014-12-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Fragment：unp residues 1-459; unp residues 537-593 Chain A 537–593（57 aa） Fragment：unp residues 1-459; unp residues 537-593	Mutation：A541T Mutation：A541T	SO4 SULFATE ION × 4 3XY 5-[(4-{[6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidin-4-yl]amino}piperidin-1-yl)methyl]-1H-indole-2-carbonitrile × 1 PG4 TETRAETHYLENE GLYCOL × 1 DMS DIMETHYL SULFOXIDE × 2 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen	Resolution 1.86 Å R-free 0.208
5DB0 Menin in complex with MI-352 Deposited 2015-08-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Fragment：UNP residues 1-459, 537-593 Chain A 537–593（57 aa） Fragment：UNP residues 1-459, 537-593	Mutation：A541T Mutation：A541T	PG4 TETRAETHYLENE GLYCOL × 3 SO4 SULFATE ION × 4 DMS DIMETHYL SULFOXIDE × 4 58P 1-[(2S)-2,3-dihydroxypropyl]-5-[(4-{[6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidin-4-yl]amino}piperidin-1-yl)methyl]-1 H-indole-2-carbonitrile × 1 6E6 1-[(2R)-2,3-dihydroxypropyl]-5-[(4-{[6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidin-4-yl]amino}piperidin-1-yl)methyl]-1H-indole-2-carbonitrile × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 1.50 Å R-free 0.185
5DB1 Menin in complex with MI-336 Deposited 2015-08-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Fragment：UNP residues 1-489, 537-593 Chain A 537–593（57 aa） Fragment：UNP residues 1-489, 537-593	Mutation：A541T Mutation：A541T	58O 6-methoxy-5-[(4-{[6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidin-4-yl]amino}piperidin-1-yl)methyl]-1H-indole-2-carbonitrile × 1 DMS DIMETHYL SULFOXIDE × 3 SO4 SULFATE ION × 5 PG4 TETRAETHYLENE GLYCOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 1.86 Å R-free 0.197
5DB2 Menin in complex with MI-389 Deposited 2015-08-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Fragment：UNP residues 1-459, 537-593 Chain A 537–593（57 aa） Fragment：UNP residues 1-459, 537-593	Mutation：A541T Mutation：A541T	58R 2-{2-cyano-5-[(4-{[6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidin-4-yl]amino}piperidin-1-yl)methyl]-1H-indol-1-yl}aceta mide × 1 DMS DIMETHYL SULFOXIDE × 3 PG4 TETRAETHYLENE GLYCOL × 1 SO4 SULFATE ION × 5 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 1.54 Å R-free 0.188
5DB3 Menin in complex with MI-574 Deposited 2015-08-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Fragment：UNP residues 1-459, 537-593 Chain A 537–593（57 aa） Fragment：UNP residues 1-459, 537-593	Mutation：A541T Mutation：A541T	DMS DIMETHYL SULFOXIDE × 3 PG4 TETRAETHYLENE GLYCOL × 2 SO4 SULFATE ION × 4 PEG DI(HYDROXYETHYL)ETHER × 1 58Q 6-methoxy-4-methyl-1-(1H-pyrazol-4-ylmethyl)-5-[(4-{[6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidin-4-yl]amino}piperidin-1-yl)methyl]-1H-indole-2-carbonitrile × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen	Resolution 1.71 Å R-free 0.194
5DD9 Menin in complex with MI-326 Deposited 2015-08-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Fragment：UNP residues 1-459, 537-593 Chain A 537–593（57 aa） Fragment：UNP residues 1-459, 537-593	Mutation：A541T Mutation：A541T	59K 4-[4-(5-methyl-1,3,4-thiadiazol-2-yl)piperazin-1-yl]-6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidine × 1 DMS DIMETHYL SULFOXIDE × 5 PG4 TETRAETHYLENE GLYCOL × 2 PGE TRIETHYLENE GLYCOL × 1 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES pH 7.5 and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl (pH 8.0), 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen, VAPOR DIFFUSION, SITTING DROP, temperature 283K	Resolution 1.62 Å R-free 0.195
5DDA Menin in complex with MI-333 Deposited 2015-08-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Fragment：UNP residues 1-459, 537-593 Chain A 537–593（57 aa） Fragment：UNP residues 1-459, 537-593	Mutation：A541T Mutation：A541T	59M 4-{4-[5-(fluoromethyl)-1,3,4-thiadiazol-2-yl]piperazin-1-yl}-6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidine × 1 DMS DIMETHYL SULFOXIDE × 4 PGE TRIETHYLENE GLYCOL × 2 EDO 1,2-ETHANEDIOL × 1 SO4 SULFATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；0.2 M ammonium acetate, 0.1 M HEPES and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen	Resolution 1.83 Å R-free 0.211
5DDB Menin in complex with MI-319 Deposited 2015-08-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Fragment：UNP residues 1-459, 537-593 Chain A 537–593（57 aa） Fragment：UNP residues 1-459, 537-593	Mutation：A541T Mutation：A541T	59Q 4-{4-[5-(difluoromethyl)-1,3,4-thiadiazol-2-yl]piperazin-1-yl}-6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidine × 1 DMS DIMETHYL SULFOXIDE × 5 PG4 TETRAETHYLENE GLYCOL × 2 PEG DI(HYDROXYETHYL)ETHER × 1 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen	Resolution 1.54 Å R-free 0.210
5DDC Menin in complex with MI-2-3 Deposited 2015-08-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Fragment：UNP residues 1-459, 537-593 Chain A 542–598（57 aa） Fragment：UNP residues 1-459, 537-593	Mutation：A541T Mutation：A541T	59V 6-(2,2,2-trifluoroethyl)-4-{4-[5-(trifluoromethyl)-1,3,4-thiadiazol-2-yl]piperazin-1-yl}thieno[2,3-d]pyrimidine × 1 DMS DIMETHYL SULFOXIDE × 4 PGE TRIETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen	Resolution 1.62 Å R-free 0.194
5DDD menin in complex with MI-836 Deposited 2015-08-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Fragment：UNP residues 1-459, 537-593 Chain A 537–593（57 aa） Fragment：UNP residues 1-459, 537-593	Not recorded	59X 4-[4-(5,5-dimethyl-4,5-dihydro-1,3-thiazol-2-yl)piperazin-1-yl]-6-(2-fluoroethyl)thieno[2,3-d]pyrimidine × 1 SO4 SULFATE ION × 4 DMS DIMETHYL SULFOXIDE × 4 PG4 TETRAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen	Resolution 2.14 Å R-free 0.248
5DDE Menin in complex with MI-859 Deposited 2015-08-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Fragment：UNP residues 1-459, 537-593 Chain A 537–593（57 aa） Fragment：UNP residues 1-459, 537-593	Mutation：A541T Mutation：A541T	5A0 6-(2,2-difluoroethyl)-4-[4-(5,5-dimethyl-4,5-dihydro-1,3-thiazol-2-yl)piperazin-1-yl]thieno[2,3-d]pyrimidine × 2 SO4 SULFATE ION × 4 DMS DIMETHYL SULFOXIDE × 4 PG4 TETRAETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen	Resolution 1.78 Å R-free 0.199
5DDF Menin in complex with MI-273 Deposited 2015-08-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Fragment：UNP residues 1-459, 537-593 Chain A 537–593（57 aa） Fragment：UNP residues 1-459, 537-593	Mutation：A541T Mutation：A541T	5A1 4-[4-(5,5-dimethyl-4,5-dihydro-1,3-thiazol-2-yl)piperazin-1-yl]-6-(pentafluoroethyl)thieno[2,3-d]pyrimidine × 1 DMS DIMETHYL SULFOXIDE × 4 PG4 TETRAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1 SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；283 K；0.2 M ammonium acetate, 0.1 M HEPES and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen	Resolution 1.66 Å R-free 0.188
6B41 Menin bound to M-525 Deposited 2017-09-25	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–610（609 aa）	Not recorded	CJV methyl {(1S,2R)-2-[(S)-cyano[1-({1-[4-({1-[4-(dimethylamino)butanoyl]azetidin-3-yl}sulfonyl)phenyl]azetidin-3-yl}methyl)piperidin-4-yl](3-fluorophenyl)methyl]cyclopentyl}carbamate × 1 7PR praseodymium triacetate × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；1.96 M NaCl, 89 mM Bis-Tris pH 6.8, 0.178 M MgCl2 and 10.7 mM Pr Acetate	Resolution 2.61 Å R-free 0.252
6BXH Menin in complex with MI-853 Deposited 2017-12-18	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa）	Not recorded	DMS DIMETHYL SULFOXIDE × 1 SO4 SULFATE ION × 1 EE7 1-{2-[4-(fluoroacetyl)piperazin-1-yl]ethyl}-4-methyl-5-[(4-{[6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidin-4-yl]amino}piperidin-1-yl)methyl]-1H-indole-2-carbonitrile × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；283 K；0.2 M ammonium acetate, 0.1 M HEPES and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen	Resolution 2.44 Å R-free 0.255
6BY8 Menin in complex with MI-1482 Deposited 2017-12-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–53（53 aa） Chain A 74–386（313 aa） Chain A 404–464（61 aa） Chain A 537–593（57 aa）	Not recorded	FNV 4-methyl-1-{[(2R)-5-oxomorpholin-2-yl]methyl}-5-[(4-{[6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidin-4-yl]amino}piperidin-1-yl)methyl]-1H-indole-2-carbonitrile × 1 DMS DIMETHYL SULFOXIDE × 4 PG4 TETRAETHYLENE GLYCOL × 2 SO4 SULFATE ION × 2 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；283 K；0.2 M ammonium acetate, 0.1 M HEPES and 25% w/v PEG 3,350. This solution was mixed 1:1 with 2.5mg/mL protein in 50mM Tris-HCl, 50mM NaCl, and 1mM TCEP. Prior to data collection, crystals were transferred into a cryo-solution containing 20% PEG550 MME and flash-frozen in liquid nitrogen	Resolution 1.90 Å R-free 0.188
6E1A Menin bound to M-89 Deposited 2018-07-09	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–610（609 aa）	Not recorded	HL7 (1S,2R)-2-[(4S)-2-methyl-4-{1-[(1-{4-[(pyridin-4-yl)sulfonyl]phenyl}azetidin-3-yl)methyl]piperidin-4-yl}-1,2,3,4-tetrahydroisoquinolin-4-yl]cyclopentyl methylcarbamate × 1 7PR praseodymium triacetate × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；2.0 M sodium chloride, 90.9 M Bis-Tris pH 6.5, 0.182 M Magnesium chloride, 9 mM Praseodymium Acetate	Resolution 3.10 Å R-free 0.235
6O5I Menin in complex with MI-3454 Deposited 2019-03-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–53（53 aa） Chain A 74–386（313 aa） Chain A 399–459（61 aa） Chain A 537–593（57 aa）	Not recorded	LMY ~{N}-[3-[[2-cyano-4-methyl-5-[[4-[[2-(methylamino)-6-[2,2,2-tris(fluoranyl)ethyl]thieno[2,3-d]pyrimidin-4-yl]amino]piperidin-1-yl]methyl]indol-1-yl]methyl]-1-bicyclo[1.1.1]pentanyl]methanamide × 1 DMS DIMETHYL SULFOXIDE × 4 SO4 SULFATE ION × 3 PG4 TETRAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, 25% (w/v) PEG-3,350.	Resolution 1.24 Å R-free 0.164
6PKC Inhibition of Human Menin by VTP-50469 Deposited 2019-06-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–457（456 aa） Chain A 552–583（32 aa）	Mutation：A5T Mutation：A5T	OP4 5-fluoro-2-({4-[7-({trans-4-[(methylsulfonyl)amino]cyclohexyl}methyl)-2,7-diazaspiro[3.5]nonan-2-yl]pyrimidin-5-yl}oxy)-N,N-di(propan-2-yl)benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；14%(w/v) PEG3350 0.2M Potassium thiocyanate 0.1M MES pH=6.0 15%(v/v) Ethylene glycol	Resolution 1.90 Å R-free 0.206
6PKC Inhibition of Human Menin by VTP-50469 Deposited 2019-06-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–457（456 aa） Chain B 552–583（32 aa）	Mutation：A5T Mutation：A5T	OP4 5-fluoro-2-({4-[7-({trans-4-[(methylsulfonyl)amino]cyclohexyl}methyl)-2,7-diazaspiro[3.5]nonan-2-yl]pyrimidin-5-yl}oxy)-N,N-di(propan-2-yl)benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；14%(w/v) PEG3350 0.2M Potassium thiocyanate 0.1M MES pH=6.0 15%(v/v) Ethylene glycol	Resolution 1.90 Å R-free 0.206
6WNH Menin bound to inhibitor M-808 Deposited 2020-04-22	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–610（609 aa）	Not recorded	7MM methyl [(1S,2R)-2-{(1S)-2-(azetidin-1-yl)-1-(3-fluorophenyl)-1-[1-({1-[4-({1-[4-(piperidin-1-yl)butanoyl]azetidin-3-yl}sulfonyl)phenyl]azetidin-3-yl}methyl)piperidin-4-yl]ethyl}cyclopentyl]carbamate × 1 7PR praseodymium triacetate × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.8；277 K；1.96 M NaCl, 89 mM Bis-Tris pH 6.8, 0.178 M MgCl2 and 10.7 mM Pr Acetate	Resolution 2.10 Å R-free 0.228
7M4T Menin bound to M-1121 Deposited 2021-03-22	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–459（458 aa） Chain A 525–615（91 aa）	Not recorded	YQV methyl {(1S,2R)-2-[(1S)-2-(azetidin-1-yl)-1-(3-fluorophenyl)-1-{1-[(3-methoxy-1-{4-[(1S,4S)-5-propanoyl-2,5-diazabicyclo[2.2.1]heptane-2-sulfonyl]phenyl}azetidin-3-yl)methyl]piperidin-4-yl}ethyl]cyclopentyl}carbamate × 1 7PR praseodymium triacetate × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；2.0 M NaCl, 90.9 M Bis-Tris pH 6.5, 0.182 M MgCl2, 10 mM Pr Acetate	Resolution 2.74 Å R-free 0.215
7OA9 Crystal structure of Human Menin in complex with Fragment 21 Deposited 2021-04-19	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–584（584 aa）	Not recorded	V6K (~{E})-2-cyano-3-(4-hydroxyphenyl)-~{N}-(2-morpholin-4-ylethyl)prop-2-enamide × 1 EDO 1,2-ETHANEDIOL × 7 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；12% PEG 3350 14% Glycerol	Resolution 2.10 Å R-free 0.235
8GPN Human menin in complex with H3K79Me2 nucleosome Deposited 2022-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 9 PDB declaration: undecameric	Chain K 1–610（610 aa）	Mutation：N-terminal Ser from cleavage of purification tag	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8IG0 Crystal structure of menin in complex with DS-1594b Deposited 2023-02-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–610（610 aa） Chain B 1–610（610 aa）	Not recorded	7IX (1R,2S,4R)-4-[[4-(5,6-dimethoxypyridazin-3-yl)phenyl]methylamino]-2-[methyl-[6-[2,2,2-tris(fluoranyl)ethyl]thieno[2,3-d]pyrimidin-4-yl]amino]cyclopentan-1-ol × 2 UNX UNKNOWN LIGAND × 2 DMS DIMETHYL SULFOXIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；283 K；0.1 M Na Cacodylate HCl, pH 6.4/ 1.5 M NaOAc/ 20 mM BaCl2. Complex crystal was prepared with soaking method.	Resolution 2.60 Å R-free 0.266
8IG0 Crystal structure of menin in complex with DS-1594b Deposited 2023-02-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–610（610 aa） Chain D 1–610（610 aa）	Not recorded	7IX (1R,2S,4R)-4-[[4-(5,6-dimethoxypyridazin-3-yl)phenyl]methylamino]-2-[methyl-[6-[2,2,2-tris(fluoranyl)ethyl]thieno[2,3-d]pyrimidin-4-yl]amino]cyclopentan-1-ol × 2 UNX UNKNOWN LIGAND × 2 DMS DIMETHYL SULFOXIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；283 K；0.1 M Na Cacodylate HCl, pH 6.4/ 1.5 M NaOAc/ 20 mM BaCl2. Complex crystal was prepared with soaking method.	Resolution 2.60 Å R-free 0.266
8VA5 Menin mutant - T349M in complex with Ziftomenib (KO-539) Deposited 2023-12-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Chain A 537–593（57 aa）	Mutation：T349M Mutation：T349M	K5O Ziftomenib × 1 PEG DI(HYDROXYETHYL)ETHER × 2 PG4 TETRAETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 1 DMS DIMETHYL SULFOXIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；285 K；0.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, 25% (w/v) PEG-3,350	Resolution 1.30 Å R-free 0.186
8VA6 Menin in complex with Ziftomenib (KO-539) Deposited 2023-12-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Chain A 537–593（57 aa）	Not recorded	K5O Ziftomenib × 1 PEG DI(HYDROXYETHYL)ETHER × 2 SO4 SULFATE ION × 3 DMS DIMETHYL SULFOXIDE × 2 PG4 TETRAETHYLENE GLYCOL × 2 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；0.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, 25% (w/v) PEG-3,350	Resolution 1.57 Å R-free 0.193
9C4S Menin mutant G331R in complex with MLL peptide Deposited 2024-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–459（459 aa） Chain A 537–593（57 aa）	Mutation：G331R Mutation：G331R	SO4 SULFATE ION × 3 1PE PENTAETHYLENE GLYCOL × 1 PG0 2-(2-METHOXYETHOXY)ETHANOL × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；285 K；0.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, 25% (w/v) PEG-3,350	Resolution 1.54 Å R-free 0.202
9C4T menin mutant M327I in complex with MLL peptide Deposited 2024-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–459（459 aa） Chain A 537–593（57 aa）	Mutation：M327I Mutation：M327I	SO4 SULFATE ION × 2 1PE PENTAETHYLENE GLYCOL × 1 PG0 2-(2-METHOXYETHOXY)ETHANOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；285 K；0.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, 25% (w/v) PEG-3,350	Resolution 1.46 Å R-free 0.184
9C4U Menin mutant T349M in complex with MLL peptide Deposited 2024-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–459（459 aa） Chain A 537–593（57 aa）	Mutation：T349M Mutation：T349M	PEG DI(HYDROXYETHYL)ETHER × 1 SO4 SULFATE ION × 1 1PE PENTAETHYLENE GLYCOL × 1 PG0 2-(2-METHOXYETHOXY)ETHANOL × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；285 K；0.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, 25% (w/v) PEG-3,350	Resolution 1.57 Å R-free 0.197
9C4V Menin mutant G331D in complex with MLL peptide Deposited 2024-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–459（459 aa） Chain A 537–593（57 aa）	Mutation：G331D Mutation：G331D	SO4 SULFATE ION × 3 1PE PENTAETHYLENE GLYCOL × 1 PG0 2-(2-METHOXYETHOXY)ETHANOL × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；285 K；0.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, 25% (w/v) PEG-3,350	Resolution 1.47 Å R-free 0.188
9C4W Menin mutant - G331R Deposited 2024-06-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Chain A 537–593（57 aa）	Mutation：G331R Mutation：G331R	PG4 TETRAETHYLENE GLYCOL × 1 SO4 SULFATE ION × 2 EDO 1,2-ETHANEDIOL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；285 K；0.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, 25% (w/v) PEG-3,350	Resolution 1.40 Å R-free 0.181
9C4X Menin mutant - M327I Deposited 2024-06-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Chain A 537–593（57 aa）	Mutation：M327I Mutation：M327I	PG4 TETRAETHYLENE GLYCOL × 2 PEG DI(HYDROXYETHYL)ETHER × 3 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；285 K；0.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, 25% (w/v) PEG-3,350	Resolution 1.58 Å R-free 0.194
9C4Y Menin mutant - T349M Deposited 2024-06-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Chain A 537–593（57 aa）	Mutation：T349M Mutation：T349M	EDO 1,2-ETHANEDIOL × 2 PG4 TETRAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；285 K；0.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, 25% (w/v) PEG-3,350	Resolution 1.31 Å R-free 0.183
9C4Z Menin mutant - G331D Deposited 2024-06-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–459（459 aa） Chain A 537–593（57 aa）	Mutation：G331D Mutation：G331D	PEG DI(HYDROXYETHYL)ETHER × 1 SO4 SULFATE ION × 2 PG4 TETRAETHYLENE GLYCOL × 2 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；285 K；0.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, 25% (w/v) PEG-3,350	Resolution 1.40 Å R-free 0.190
9C92 Crystal structure of menin in complex with inhibitor compound 15 Deposited 2024-06-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–457（456 aa） Chain A 552–583（32 aa）	Mutation：A5T Mutation：A5T	A1AVE N-ethyl-5-fluoro-2-[(5-{7-[(1-methylcyclopropyl)methyl]-2,7-diazaspiro[3.5]nonan-2-yl}-1,2,4-triazin-6-yl)oxy]-N-(propan-2-yl)benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；20% PEG 3350, 0.1M HEPES pH6.9, 0.2M Na Thiocyanate, 1% Tacsimate, 4% Isopropanol	Resolution 1.90 Å R-free 0.244
9C92 Crystal structure of menin in complex with inhibitor compound 15 Deposited 2024-06-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–457（456 aa） Chain B 552–583（32 aa）	Mutation：A5T Mutation：A5T	A1AVE N-ethyl-5-fluoro-2-[(5-{7-[(1-methylcyclopropyl)methyl]-2,7-diazaspiro[3.5]nonan-2-yl}-1,2,4-triazin-6-yl)oxy]-N-(propan-2-yl)benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；20% PEG 3350, 0.1M HEPES pH6.9, 0.2M Na Thiocyanate, 1% Tacsimate, 4% Isopropanol	Resolution 1.90 Å R-free 0.244
9C93 Crystal structure of menin in complex with inhibitor compound 26 Deposited 2024-06-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–457（456 aa） Chain A 552–583（32 aa）	Mutation：A5T Mutation：A5T	A1AVF (1R,5R)-2-({5-fluoro-2-[(5-{7-[(1-methylcyclopropyl)methyl]-2,7-diazaspiro[3.5]nonan-2-yl}-1,2,4-triazin-6-yl)oxy]phenyl}methyl)-2-azabicyclo[3.1.0]hexan-3-one × 1 K POTASSIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；18% PEG 3350, 0.1M HEPES pH6.9, 0.2M K Thiocyanate, 4% Isopropanol, 1% Tacsimate	Resolution 1.85 Å R-free 0.225
9C93 Crystal structure of menin in complex with inhibitor compound 26 Deposited 2024-06-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–457（456 aa） Chain B 552–583（32 aa）	Mutation：A5T Mutation：A5T	A1AVF (1R,5R)-2-({5-fluoro-2-[(5-{7-[(1-methylcyclopropyl)methyl]-2,7-diazaspiro[3.5]nonan-2-yl}-1,2,4-triazin-6-yl)oxy]phenyl}methyl)-2-azabicyclo[3.1.0]hexan-3-one × 1 K POTASSIUM ION × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；18% PEG 3350, 0.1M HEPES pH6.9, 0.2M K Thiocyanate, 4% Isopropanol, 1% Tacsimate	Resolution 1.85 Å R-free 0.225
9C94 Crystal structure of menin in complex with inhibitor compound 20 Deposited 2024-06-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–457（456 aa） Chain A 552–583（32 aa）	Mutation：A5T Mutation：A5T	A1AVG {5-fluoro-2-[(5-{7-[(1-methylcyclopropyl)methyl]-2,7-diazaspiro[3.5]nonan-2-yl}-1,2,4-triazin-6-yl)oxy]phenyl}[(1R,5S)-3-oxa-8-azabicyclo[3.2.1]octan-8-yl]methanone × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；22% PEG 3350, 0.1M HEPES pH6.9, 0.2M Na Thiocyanate, 4% Isopropanol, 1% Tacsimate	Resolution 1.98 Å R-free 0.212
9C94 Crystal structure of menin in complex with inhibitor compound 20 Deposited 2024-06-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–457（456 aa） Chain B 552–583（32 aa）	Mutation：A5T Mutation：A5T	A1AVG {5-fluoro-2-[(5-{7-[(1-methylcyclopropyl)methyl]-2,7-diazaspiro[3.5]nonan-2-yl}-1,2,4-triazin-6-yl)oxy]phenyl}[(1R,5S)-3-oxa-8-azabicyclo[3.2.1]octan-8-yl]methanone × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；22% PEG 3350, 0.1M HEPES pH6.9, 0.2M Na Thiocyanate, 4% Isopropanol, 1% Tacsimate	Resolution 1.98 Å R-free 0.212
9WKU Wild-type Menin complexed with JNJ-75276617 Deposited 2025-09-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–457（456 aa） Chain A 551–583（33 aa）	Not recorded	9N6 N-ethyl-5-fluoro-2-{[5-(2-{(3R)-6-[(2-methoxyethyl)(methyl)amino]-2-methylhexan-3-yl}-2,6-diazaspiro[3.4]octan-6-yl)-1,2,4-triazin-6-yl]oxy}-N-(propan-2-yl)benzamide × 1 EDO 1,2-ETHANEDIOL × 2 MG MAGNESIUM ION × 1 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；22%(w/v) PEG3350, 0.2M MAGNESIUM NITRATE, 0.1 M HEPES PH=7.8, 20%(v/v) ETHYLENE GLYCOL, PH7.8	Resolution 1.90 Å R-free 0.204
9WKU Wild-type Menin complexed with JNJ-75276617 Deposited 2025-09-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–457（456 aa） Chain B 551–583（33 aa）	Not recorded	9N6 N-ethyl-5-fluoro-2-{[5-(2-{(3R)-6-[(2-methoxyethyl)(methyl)amino]-2-methylhexan-3-yl}-2,6-diazaspiro[3.4]octan-6-yl)-1,2,4-triazin-6-yl]oxy}-N-(propan-2-yl)benzamide × 1 EDO 1,2-ETHANEDIOL × 2 MG MAGNESIUM ION × 2 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；22%(w/v) PEG3350, 0.2M MAGNESIUM NITRATE, 0.1 M HEPES PH=7.8, 20%(v/v) ETHYLENE GLYCOL, PH7.8	Resolution 1.90 Å R-free 0.204
9WKV [M322I] Menin complexed with JNJ-75276617 Deposited 2025-09-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–457（456 aa） Chain A 551–583（33 aa）	Not recorded	9N6 N-ethyl-5-fluoro-2-{[5-(2-{(3R)-6-[(2-methoxyethyl)(methyl)amino]-2-methylhexan-3-yl}-2,6-diazaspiro[3.4]octan-6-yl)-1,2,4-triazin-6-yl]oxy}-N-(propan-2-yl)benzamide × 1 EDO 1,2-ETHANEDIOL × 2 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；18%(w/v) PEG3350, 0.2 M POTASIUM THIOCYANATE, 0.1M MES PH=6.2, 20%(v/v) ETHYLENE GLYCOL, PH 6.2	Resolution 1.80 Å R-free 0.198
9WKV [M322I] Menin complexed with JNJ-75276617 Deposited 2025-09-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–457（456 aa） Chain B 551–583（33 aa）	Not recorded	9N6 N-ethyl-5-fluoro-2-{[5-(2-{(3R)-6-[(2-methoxyethyl)(methyl)amino]-2-methylhexan-3-yl}-2,6-diazaspiro[3.4]octan-6-yl)-1,2,4-triazin-6-yl]oxy}-N-(propan-2-yl)benzamide × 1 EDO 1,2-ETHANEDIOL × 4 MG MAGNESIUM ION × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；18%(w/v) PEG3350, 0.2 M POTASIUM THIOCYANATE, 0.1M MES PH=6.2, 20%(v/v) ETHYLENE GLYCOL, PH 6.2	Resolution 1.80 Å R-free 0.198
9WKW Wild-type Menin complexed with DS-1594 Deposited 2025-09-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–457（456 aa） Chain A 551–583（33 aa）	Not recorded	7IX (1R,2S,4R)-4-[[4-(5,6-dimethoxypyridazin-3-yl)phenyl]methylamino]-2-[methyl-[6-[2,2,2-tris(fluoranyl)ethyl]thieno[2,3-d]pyrimidin-4-yl]amino]cyclopentan-1-ol × 1 EDO 1,2-ETHANEDIOL × 6 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；22%(w/v) PEG3350, 0.2M MAGNESIUM NITRATE, 0.1 M HEPES PH=7.8, 20%(v/v) ETHYLENE GLYCOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K	Resolution 1.63 Å R-free 0.176
9WKW Wild-type Menin complexed with DS-1594 Deposited 2025-09-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–457（456 aa） Chain B 551–583（33 aa）	Not recorded	7IX (1R,2S,4R)-4-[[4-(5,6-dimethoxypyridazin-3-yl)phenyl]methylamino]-2-[methyl-[6-[2,2,2-tris(fluoranyl)ethyl]thieno[2,3-d]pyrimidin-4-yl]amino]cyclopentan-1-ol × 1 EDO 1,2-ETHANEDIOL × 9 NA SODIUM ION × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；22%(w/v) PEG3350, 0.2M MAGNESIUM NITRATE, 0.1 M HEPES PH=7.8, 20%(v/v) ETHYLENE GLYCOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K	Resolution 1.63 Å R-free 0.176
9WKX [M322I] Menin complexed with DS-1594 Deposited 2025-09-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–457（456 aa） Chain A 551–583（33 aa）	Not recorded	7IX (1R,2S,4R)-4-[[4-(5,6-dimethoxypyridazin-3-yl)phenyl]methylamino]-2-[methyl-[6-[2,2,2-tris(fluoranyl)ethyl]thieno[2,3-d]pyrimidin-4-yl]amino]cyclopentan-1-ol × 1 EDO 1,2-ETHANEDIOL × 2 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；19%(w/v) PEG3350, 0.2 M POTASIUM THIOCYANATE, 0.1 M MES PH=6.3, 20%(v/v) ETHYLENE GLYCOL, PH 6.5	Resolution 2.25 Å R-free 0.239
9WKX [M322I] Menin complexed with DS-1594 Deposited 2025-09-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–457（456 aa） Chain B 551–583（33 aa）	Not recorded	7IX (1R,2S,4R)-4-[[4-(5,6-dimethoxypyridazin-3-yl)phenyl]methylamino]-2-[methyl-[6-[2,2,2-tris(fluoranyl)ethyl]thieno[2,3-d]pyrimidin-4-yl]amino]cyclopentan-1-ol × 1 EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；19%(w/v) PEG3350, 0.2 M POTASIUM THIOCYANATE, 0.1 M MES PH=6.3, 20%(v/v) ETHYLENE GLYCOL, PH 6.5	Resolution 2.25 Å R-free 0.239
9WN9 Wild-type Menin complexed with DSP-5336 Deposited 2025-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–457（456 aa） Chain A 551–583（33 aa）	Not recorded	2IZ 5-fluoro-2-[(4-{7-[(1S,3S,4R)-5-methylidene-2-azabicyclo[2.2.2]octane-3-carbonyl]-2,7-diazaspiro[3.5]nonan-2-yl}pyrimidin-5-yl)oxy]-N,N-di(propan-2-yl)benzamide × 1 EDO 1,2-ETHANEDIOL × 1 MG MAGNESIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；18%(w/v) PEG3350, 0.2M POTASIUM THIOCYANATE, 0.1 M MES PH=6.0, 20%(v/v) ETHYLENE GLYCOL, PH 6.0	Resolution 1.50 Å R-free 0.214
9WN9 Wild-type Menin complexed with DSP-5336 Deposited 2025-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–457（456 aa） Chain B 551–583（33 aa）	Not recorded	2IZ 5-fluoro-2-[(4-{7-[(1S,3S,4R)-5-methylidene-2-azabicyclo[2.2.2]octane-3-carbonyl]-2,7-diazaspiro[3.5]nonan-2-yl}pyrimidin-5-yl)oxy]-N,N-di(propan-2-yl)benzamide × 1 EDO 1,2-ETHANEDIOL × 2 MG MAGNESIUM ION × 3 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；18%(w/v) PEG3350, 0.2M POTASIUM THIOCYANATE, 0.1 M MES PH=6.0, 20%(v/v) ETHYLENE GLYCOL, PH 6.0	Resolution 1.50 Å R-free 0.214
9WNA [M322I] Menin complexed with DSP-5336 Deposited 2025-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–457（456 aa） Chain A 551–583（33 aa）	Not recorded	2IZ 5-fluoro-2-[(4-{7-[(1S,3S,4R)-5-methylidene-2-azabicyclo[2.2.2]octane-3-carbonyl]-2,7-diazaspiro[3.5]nonan-2-yl}pyrimidin-5-yl)oxy]-N,N-di(propan-2-yl)benzamide × 1 EDO 1,2-ETHANEDIOL × 3 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；18%(w/v) PEG3350, 0.2M POTASIUM THIOCYANATE, 0.1M MES PH=6.0, 20%(v/v) ETHYLENE GLYCOL, PH 6.0	Resolution 2.00 Å R-free 0.212
9WNA [M322I] Menin complexed with DSP-5336 Deposited 2025-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–457（456 aa） Chain B 551–583（33 aa）	Not recorded	2IZ 5-fluoro-2-[(4-{7-[(1S,3S,4R)-5-methylidene-2-azabicyclo[2.2.2]octane-3-carbonyl]-2,7-diazaspiro[3.5]nonan-2-yl}pyrimidin-5-yl)oxy]-N,N-di(propan-2-yl)benzamide × 1 EDO 1,2-ETHANEDIOL × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；18%(w/v) PEG3350, 0.2M POTASIUM THIOCYANATE, 0.1M MES PH=6.0, 20%(v/v) ETHYLENE GLYCOL, PH 6.0	Resolution 2.00 Å R-free 0.212
9WNI Wild-type Menin complexed with KO-539 Deposited 2025-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–457（456 aa） Chain A 551–583（33 aa）	Not recorded	K5O Ziftomenib × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；24%(w/v) PEG3350, 0.2M MAGNESIUM NITRATE, 0.1M HEPES PH=7.8, 20%(v/v) ETHYLENE GLYCOL, PH7.8	Resolution 2.40 Å R-free 0.275
9WNI Wild-type Menin complexed with KO-539 Deposited 2025-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–457（456 aa） Chain B 551–583（33 aa）	Not recorded	K5O Ziftomenib × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；24%(w/v) PEG3350, 0.2M MAGNESIUM NITRATE, 0.1M HEPES PH=7.8, 20%(v/v) ETHYLENE GLYCOL, PH7.8	Resolution 2.40 Å R-free 0.275
9WNJ [M322I] Menin complexed with KO-539 Deposited 2025-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–457（456 aa） Chain A 551–583（33 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 2 K5O Ziftomenib × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；19%(w/v) PEG3350, 0.2M POTASIUM THIOCYANATE, 0.1M MES PH=6.2, 20%(v/v) ETHYLENE GLYCOL, PH 6.2	Resolution 2.00 Å R-free 0.207
9WNJ [M322I] Menin complexed with KO-539 Deposited 2025-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–457（456 aa） Chain B 551–583（33 aa）	Not recorded	K5O Ziftomenib × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；19%(w/v) PEG3350, 0.2M POTASIUM THIOCYANATE, 0.1M MES PH=6.2, 20%(v/v) ETHYLENE GLYCOL, PH 6.2	Resolution 2.00 Å R-free 0.207

60 other PDB entries and 77 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MEN1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–539； UniProt 2–610 Author chain B； PDBConstruct 3–539； UniProt 2–610 Author chain C； PDBConstruct 3–539； UniProt 2–610 Author chain D； PDBConstruct 3–539； UniProt 2–610

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9z4x
Deposition date deposition_date	2025-11-11
最后修订 last_revision	2025-11-26
Structure title title	MENIN IN COMPLEX WITH JNJ-75276617 (Bleximenib)
Keywords keywords	MENIN, MEN1, MLL, TRANSCRIPTION, INHIBITOR COMPLEX, Bleximenib, TRANSCRIPTION-INHIBITOR complex; TRANSCRIPTION/INHIBITOR
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	49.28 Å
Radius of gyration Rg (electron density) rg_electron	49.51 Å
Forward intensity I(0) i0	1343060000.00
Molecular weight molecular_weight	203590.0 kDa
Excluded volume excluded_volume	197910 Å³
Envelope volume envelope_volume	405520 Å³
Hydration-shell volume shell_volume	70155 Å³
Envelope diameter envelope_diameter	189.5 Å
Shell Rg shell_rg	50.40 Å
Envelope Rg envelope_rg	49.17 Å
Shape Rg shape_rg	49.50 Å
Total Rg total_rg	49.54 Å
Total atoms total_atoms	15463
Residues n_residues	1936
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	178.2 Å
Rg (real space) rg_real	49.66 Å
Rg uncertainty (real space) rg_real_error	2.35 Å
I(0) (real space) i0_real	1.3430e+09
I(0) uncertainty (real space) i0_real_error	2.6830e+07
Rg (reciprocal space) rg_reciprocal	49.29 Å
I(0) (reciprocal space) i0_reciprocal	1342000000.0000
Solution quality estimate total_estimate	0.7739
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	50.1 Å
Skewness Skewness skewness	0.454
Kurtosis Kurtosis kurtosis	-0.425
Angular range angular_range	— – 0.1600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	53180000.0000
Real-space data points n_real_points	33
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.728; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.871; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	Menin
Molecular weight formula_weight	59790.0 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	15547

GSGLKAAQKTLFPLRSIDDVVRLFAAELGREEPDLVLLSLVLGFVEHFLAVNRVIPTNVPELTFQPSPAPDPPGGLTYFPVADLSIIAALYARFTAQIRGAVDLSLYPREGGVSSRELVKKVSDVIWNSLSRSYFKDRAHIQSLFSFITGTKLDSSGVAFAVVGACQALGLRDVHLALSEDHAWVVFGPNGEQTAEVTWHGKGNEDRRGQTVNAGVAERSWLYLKGSYMRCDRKMEVAFMVCAINPSIDLHTDSLELLQLQQKLLWLLYDLGHLERYPMALGNLADLEELEPTPGRPDPLTLYHKGIASAKTYYRDEHIYPYMYLAGYHCRNRNVREALQAWADTATVIQDYNYCREDEEIYKEFFEVANDVIPNLLKEAASLLEAGSQGSALQDPECFAHLLRFYDGICKWEEGSPTPVLHVGWATFLVQSLGRFEGQVRQKVRIVSGTVAGTARGPEGGSTAQVPAPTASPPPEGPVLTFQSEKMKGMKELLVATKINSSAIKLQLTAQSQVQMKKQKVSTPSDYTLSFLKRQRKGL

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	BETA-MERCAPTOETHANOL
Molecular weight formula_weight	78.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	;N-ethyl-5-fluoro-2-{[5-(2-{(3R)-6-[(2-methoxyethyl)(methyl)amino]-2-methylhexan-3-yl}-2,6-diazaspiro[3.4]octan-6-yl)-1,2,4-triazin-6-yl]oxy}-N-(propan-2-yl)benzamide ;
Molecular weight formula_weight	599.8 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 5 Entity 5 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 6 Entity 6 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	84

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8. Citations (1)

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Unit-cell length a length_a	143.372 Å
Unit-cell length b length_b	70.486 Å
Unit-cell length c length_c	145.561 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.68 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.950 Å
Low-resolution limit resolution_low	145.500 Å
R factor r_factor	0.2366
R_work r_work	0.2333
R_free r_free	0.2969

fit	/app/data/saxs_computation/z4/9z4x/9z4x.fit
pddf	/app/data/pr_computation/z4/9z4x/9z4x.pr.out
profile	/app/data/saxs_computation/z4/9z4x/9z4x.dat