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- PDB-37bg: Crystal Structure of Histone-lysine N-methyltransferase from Leis... -

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Basic information

Entry
Database: PDB / ID: 37bg
TitleCrystal Structure of Histone-lysine N-methyltransferase from Leishmania major in complex with S-ADENOSYLMETHIONINE
ComponentsHistone-lysine N-methyltransferase, H3 lysine-79 specific
KeywordsTRANSFERASE / SSGCID / STRUCTURAL GENOMICS / SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE / Histone-lysine N-methyltransferase / Leishmania major
Function / homology
Function and homology information


histone H3K79 trimethyltransferase activity / histone H3K79 methyltransferase activity / subtelomeric heterochromatin formation / DNA damage checkpoint signaling / methylation / chromosome, telomeric region / DNA repair / nucleus
Similarity search - Function
Histone-lysine N-methyltransferase DOT1 domain / Histone H3-K79 methyltransferase / Histone methylation protein DOT1 / Histone-lysine N-methyltransferase DOT1 (EC 2.1.1.43) domain profile. / S-adenosyl-L-methionine-dependent methyltransferase superfamily
Similarity search - Domain/homology
S-ADENOSYLMETHIONINE / Histone-lysine N-methyltransferase, H3 lysine-79 specific
Similarity search - Component
Biological speciesLeishmania major strain Friedlin (eukaryote)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.93 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID)
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)75N93022C00036 United States
CitationJournal: To be published
Title: Crystal Structure of Histone-lysine N-methyltransferase from Leishmania major in complex with S-ADENOSYLMETHIONINE
Authors: Lanyi Lari, N. / Liu, L. / Lovell, S. / Battaile, K.P.
History
DepositionJul 10, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 22, 2026Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Histone-lysine N-methyltransferase, H3 lysine-79 specific
B: Histone-lysine N-methyltransferase, H3 lysine-79 specific
C: Histone-lysine N-methyltransferase, H3 lysine-79 specific
D: Histone-lysine N-methyltransferase, H3 lysine-79 specific
hetero molecules


Theoretical massNumber of molelcules
Total (without water)121,40717
Polymers118,5204
Non-polymers2,88713
Water10,881604
1
A: Histone-lysine N-methyltransferase, H3 lysine-79 specific
hetero molecules


Theoretical massNumber of molelcules
Total (without water)30,3034
Polymers29,6301
Non-polymers6733
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Histone-lysine N-methyltransferase, H3 lysine-79 specific
hetero molecules


Theoretical massNumber of molelcules
Total (without water)30,3034
Polymers29,6301
Non-polymers6733
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Histone-lysine N-methyltransferase, H3 lysine-79 specific
hetero molecules


Theoretical massNumber of molelcules
Total (without water)30,4975
Polymers29,6301
Non-polymers8674
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: Histone-lysine N-methyltransferase, H3 lysine-79 specific
hetero molecules


Theoretical massNumber of molelcules
Total (without water)30,3034
Polymers29,6301
Non-polymers6733
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)69.816, 91.915, 81.797
Angle α, β, γ (deg.)90.00, 102.67, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Histone-lysine N-methyltransferase, H3 lysine-79 specific / Histone H3-K76 methyltransferase / Histone H3-K79 methyltransferase / Histone-lysine N- ...Histone H3-K76 methyltransferase / Histone H3-K79 methyltransferase / Histone-lysine N-methyltransferase / H3 lysine-76 specific


Mass: 29630.020 Da / Num. of mol.: 4 / Fragment: E50-K299
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Leishmania major strain Friedlin (eukaryote)
Gene: LMJF_07_0025 / Plasmid: LemaA.18205.a.B2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q4QIU2

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Non-polymers , 5 types, 617 molecules

#2: Chemical
ChemComp-SAM / S-ADENOSYLMETHIONINE


Mass: 398.437 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C15H22N6O5S / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-BTB / 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / BIS-TRIS BUFFER


Mass: 209.240 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C8H19NO5 / Comment: pH buffer*YM
#5: Chemical ChemComp-PG4 / TETRAETHYLENE GLYCOL


Mass: 194.226 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 604 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.16 Å3/Da / Density % sol: 43.07 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: 27.5% PEG 3350, 0.1M Bis-Tris 5.5, 0.2M NaCl. LemaA.18205.a.B2.PW39520 at 12.4 mg/mL. Crystals soaked with 5 mM SAM, plate 21007 C10 drop 2, Puck: PSL-2811, Cryo: 33% P3350, 0.1M BT 5.5, 0.2M NaCl

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NSLS-II / Beamline: 19-ID / Wavelength: 0.9786 Å
DetectorType: DECTRIS EIGER2 XE 9M / Detector: PIXEL / Date: Jun 13, 2026
RadiationMonochromator: Double Crystal Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9786 Å / Relative weight: 1
ReflectionResolution: 1.93→49.37 Å / Num. obs: 75739 / % possible obs: 99.9 % / Redundancy: 6.8 % / CC1/2: 0.997 / Rmerge(I) obs: 0.145 / Rpim(I) all: 0.06 / Rrim(I) all: 0.157 / Χ2: 1.01 / Net I/σ(I): 8.1 / Num. measured all: 516275
Reflection shellResolution: 1.93→1.97 Å / % possible obs: 99.9 % / Redundancy: 5.6 % / Rmerge(I) obs: 1.095 / Num. measured all: 24871 / Num. unique obs: 4461 / CC1/2: 0.728 / Rpim(I) all: 0.504 / Rrim(I) all: 1.21 / Χ2: 1.04 / Net I/σ(I) obs: 1.5

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Processing

Software
NameVersionClassification
PHENIX(2.1_6048: ???)refinement
Aimlessdata scaling
XDSdata reduction
PHASERphasing
PDB_EXTRACTdata extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.93→49.37 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 27.19 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2313 3706 4.9 %
Rwork0.1826 --
obs0.1851 75562 99.71 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.93→49.37 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8067 0 181 604 8852
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0078534
X-RAY DIFFRACTIONf_angle_d0.91411579
X-RAY DIFFRACTIONf_dihedral_angle_d15.7333253
X-RAY DIFFRACTIONf_chiral_restr0.0511260
X-RAY DIFFRACTIONf_plane_restr0.0111493
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.93-1.960.37191400.31582771X-RAY DIFFRACTION100
1.96-1.980.28061420.28672745X-RAY DIFFRACTION100
1.98-2.010.30131650.26622709X-RAY DIFFRACTION100
2.01-2.040.29571560.24962752X-RAY DIFFRACTION100
2.04-2.070.2581530.21622739X-RAY DIFFRACTION100
2.07-2.110.28491620.21412732X-RAY DIFFRACTION100
2.11-2.140.25141290.20952767X-RAY DIFFRACTION100
2.14-2.180.26661330.20522785X-RAY DIFFRACTION100
2.18-2.220.27261400.20062735X-RAY DIFFRACTION100
2.22-2.270.24381390.20022772X-RAY DIFFRACTION100
2.27-2.320.24061290.18932775X-RAY DIFFRACTION100
2.32-2.370.31161490.19462734X-RAY DIFFRACTION100
2.37-2.430.2411250.18592769X-RAY DIFFRACTION100
2.43-2.50.27631520.19272784X-RAY DIFFRACTION100
2.5-2.570.23991500.18332733X-RAY DIFFRACTION100
2.57-2.650.24371230.18372765X-RAY DIFFRACTION99
2.65-2.750.22041060.18042766X-RAY DIFFRACTION100
2.75-2.860.23321320.18462775X-RAY DIFFRACTION100
2.86-2.990.24391510.18542752X-RAY DIFFRACTION100
2.99-3.150.24841330.19662800X-RAY DIFFRACTION100
3.15-3.340.25891380.18052753X-RAY DIFFRACTION100
3.34-3.60.20431540.16162770X-RAY DIFFRACTION100
3.6-3.960.20221430.15322786X-RAY DIFFRACTION100
3.96-4.540.16921620.132776X-RAY DIFFRACTION100
4.54-5.710.17971550.15032777X-RAY DIFFRACTION100
5.71-49.370.21821450.19022834X-RAY DIFFRACTION99
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.10190.36680.51064.0501-0.02273.8943-0.0051-0.55920.88630.43120.03260.0663-0.18050.0697-0.02620.23230.05320.04140.2062-0.04290.4475-2.542118.591510.9566
22.0829-1.4062-1.31393.98321.01972.5688-0.051-0.09120.3286-0.02690.0604-0.0882-0.14390.0140.00780.1411-0.0197-0.03260.1470.01050.350712.00526.592.7431
31.5239-0.3904-0.17742.410.54392.0759-0.0603-0.06420.08520.16050.1488-0.03530.00330.1395-0.06820.1290.01990.00960.1635-0.01630.248211.9766-5.68697.2599
42.6590.6979-0.63491.93650.94671.8918-0.02650.0257-0.40130.1133-0.01050.59960.1584-0.15960.00620.16460.02030.01380.18670.02040.459-5.506-7.74926.7957
54.27890.4692-0.95650.0573-0.131.08740.04670.1966-0.41320.06520.21170.49190.0542-0.2576-0.15540.1547-0.00210.04140.25730.07090.6571-17.87992.7944.4024
65.40991.2173-2.15731.9765-1.37833.2705-0.0461-0.0328-0.05070.20620.00870.40250.0055-0.12630.0140.16190.01980.03670.1642-0.01850.3849-5.35187.41666.2695
72.73691.1547-1.4666.4022-0.62188.1303-0.0601-0.87511.04630.5062-0.05460.4179-0.2412-0.05110.1340.2460.02970.00390.2323-0.04830.396-11.977421.909950.8862
83.2088-1.3679-0.56593.34891.19863.0790.0162-0.01330.2004-0.2495-0.0119-0.0875-0.0356-0.10060.00740.21-0.0131-0.00360.19180.010.24932.958611.080341.9365
94.9678-0.6434-0.19914.44330.8233.94020.0991-0.1996-0.2588-0.08950.0631-0.20380.01210.0206-0.17070.20970.0255-0.01350.18220.030.26193.6853-0.482646.499
104.519-1.6061-0.02680.9356-0.25660.66090.0444-0.0314-0.7201-0.04880.02190.42220.1173-0.0445-0.06360.291-0.0183-0.05030.26570.01830.4253-13.5016-2.192545.699
113.26980.0353-1.0562.3202-0.85042.4288-0.0651-0.05220.0187-0.00960.03170.1903-0.0387-0.2083-0.01460.1950.0067-0.05550.295-0.02020.2808-14.708810.929545.3954
124.4861-4.99251.34815.5925-1.49574.0458-0.1630.6834-0.2175-0.67140.0825-0.46320.24710.14670.0520.2986-0.06390.00140.2192-0.05090.5949-37.1221.4383-10.6153
132.3935-0.76760.69136.86521.14110.4852-0.33990.3966-1.0013-0.51870.4803-0.6370.09130.2526-0.14010.3414-0.02510.1480.3194-0.16150.8027-22.17673.1847-12.4691
143.53950.0358-0.11552.15841.70352.9024-0.141-0.0697-0.29050.03780.0702-0.33010.18330.30530.05380.19250.0261-0.01410.14580.03410.3598-18.079418.28613.2294
151.68930.5925-0.20532.11010.33861.016-0.09810.1202-0.0437-0.12440.1052-0.1332-0.00870.0942-0.00220.1294-0.00670.01480.1606-0.01320.2641-24.21623.7251-5.8485
161.68620.22420.5671.64550.49661.3345-0.012-0.01710.1708-0.08370.01460.5125-0.1428-0.0516-0.01710.1329-0.01710.00750.1729-0.00840.3776-40.689727.8898-6.0915
174.5913-0.41581.07351.4992-1.03610.93460.01320.007-0.2725-0.18170.06940.22340.1163-0.1245-0.06480.161-0.0250.00690.1877-0.0160.3152-44.234514.3067-4.9021
180.5392-0.0717-0.67843.81061.04711.1854-0.38780.433-1.254-0.16460.1947-0.46230.1423-0.05440.14460.2825-0.02020.03420.3037-0.0790.4895-39.65096.224627.9813
192.43130.36170.69112.97360.19431.22420.0406-0.1096-0.1620.2672-0.0421-0.1687-0.00560.06260.01110.2167-0.02140.02190.23420.00160.2383-31.988526.427135.6157
201.8752-0.72031.69543.4502-1.0844.73570.00530.07750.27910.07120.02670.3553-0.2527-0.0779-0.0730.1832-0.01230.04570.2617-0.00270.3354-49.33831.738933.2032
215.5188-0.29890.4012.311-0.67182.0882-0.0443-0.22040.16130.09870.07770.3109-0.0389-0.3206-0.03820.1961-0.01310.03910.2504-0.01280.2174-53.307318.16633.8943
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 48 through 67 )
2X-RAY DIFFRACTION2chain 'A' and (resid 68 through 127 )
3X-RAY DIFFRACTION3chain 'A' and (resid 128 through 203 )
4X-RAY DIFFRACTION4chain 'A' and (resid 204 through 249 )
5X-RAY DIFFRACTION5chain 'A' and (resid 250 through 266 )
6X-RAY DIFFRACTION6chain 'A' and (resid 267 through 299 )
7X-RAY DIFFRACTION7chain 'B' and (resid 46 through 65 )
8X-RAY DIFFRACTION8chain 'B' and (resid 66 through 127 )
9X-RAY DIFFRACTION9chain 'B' and (resid 128 through 186 )
10X-RAY DIFFRACTION10chain 'B' and (resid 187 through 265 )
11X-RAY DIFFRACTION11chain 'B' and (resid 266 through 299 )
12X-RAY DIFFRACTION12chain 'C' and (resid 48 through 67 )
13X-RAY DIFFRACTION13chain 'C' and (resid 68 through 82 )
14X-RAY DIFFRACTION14chain 'C' and (resid 83 through 108 )
15X-RAY DIFFRACTION15chain 'C' and (resid 109 through 203 )
16X-RAY DIFFRACTION16chain 'C' and (resid 204 through 249 )
17X-RAY DIFFRACTION17chain 'C' and (resid 250 through 299 )
18X-RAY DIFFRACTION18chain 'D' and (resid 49 through 82 )
19X-RAY DIFFRACTION19chain 'D' and (resid 83 through 203 )
20X-RAY DIFFRACTION20chain 'D' and (resid 204 through 249 )
21X-RAY DIFFRACTION21chain 'D' and (resid 250 through 299 )

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