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- PDB-6f3o: Crystal structure of S-adenosyl-L-homocysteine hydrolase from Pse... -

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Basic information

Entry
Database: PDB / ID: 6f3o
TitleCrystal structure of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa complexed with adenine, K+ and Zn2+ cations
ComponentsAdenosylhomocysteinase
KeywordsHYDROLASE / REGULATION OF SAM-DEPENDENT METHYLATION REACTIONS
Function / homology
Function and homology information


adenosylhomocysteinase / S-adenosylmethionine cycle / adenosylhomocysteinase activity / one-carbon metabolic process / cytosol
Similarity search - Function
Adenosylhomocysteinase-like / Adenosylhomocysteinase-like / S-adenosyl-L-homocysteine hydrolase, conserved site / Adenosylhomocysteinase-like superfamily / S-adenosyl-L-homocysteine hydrolase, NAD binding domain / S-adenosyl-L-homocysteine hydrolase / S-adenosyl-L-homocysteine hydrolase signature 1. / S-adenosyl-L-homocysteine hydrolase signature 2. / S-adenosyl-L-homocysteine hydrolase / S-adenosyl-L-homocysteine hydrolase, NAD binding domain ...Adenosylhomocysteinase-like / Adenosylhomocysteinase-like / S-adenosyl-L-homocysteine hydrolase, conserved site / Adenosylhomocysteinase-like superfamily / S-adenosyl-L-homocysteine hydrolase, NAD binding domain / S-adenosyl-L-homocysteine hydrolase / S-adenosyl-L-homocysteine hydrolase signature 1. / S-adenosyl-L-homocysteine hydrolase signature 2. / S-adenosyl-L-homocysteine hydrolase / S-adenosyl-L-homocysteine hydrolase, NAD binding domain / S-adenosyl-L-homocysteine hydrolase, NAD binding domain / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ADENINE / : / NICOTINAMIDE-ADENINE-DINUCLEOTIDE / PHOSPHATE ION / Adenosylhomocysteinase
Similarity search - Component
Biological speciesPseudomonas aeruginosa (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.75 Å
AuthorsCzyrko, J. / Brzezinski, K.
Funding support Poland, 1items
OrganizationGrant numberCountry
National Science Centre, PolandUMO-2013/09/B/NZ1/01880 Poland
CitationJournal: Sci Rep / Year: 2018
Title: Metal-cation regulation of enzyme dynamics is a key factor influencing the activity of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa.
Authors: Czyrko, J. / Sliwiak, J. / Imiolczyk, B. / Gdaniec, Z. / Jaskolski, M. / Brzezinski, K.
History
DepositionNov 28, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 8, 2018Provider: repository / Type: Initial release
Revision 1.1Jan 17, 2024Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / struct_conn / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_label_alt_id / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Adenosylhomocysteinase
B: Adenosylhomocysteinase
C: Adenosylhomocysteinase
D: Adenosylhomocysteinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)211,27327
Polymers206,9404
Non-polymers4,33323
Water29,1121616
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration, light scattering
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area30740 Å2
ΔGint-178 kcal/mol
Surface area57110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)170.839, 99.614, 111.825
Angle α, β, γ (deg.)90.00, 101.97, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14B
24C
15B
25D
16C
26D

NCS domain segments:

Component-ID: 0 / Beg auth comp-ID: PHE / Beg label comp-ID: PHE / Refine code: 0

Dom-IDEns-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11TYRTYRAA10 - 46913 - 472
21TYRTYRBB10 - 46913 - 472
12TYRTYRAA10 - 46913 - 472
22TYRTYRCC10 - 46913 - 472
13ARGARGAA10 - 46813 - 471
23ARGARGDD10 - 46813 - 471
14TYRTYRBB10 - 46913 - 472
24TYRTYRCC10 - 46913 - 472
15ARGARGBB10 - 46813 - 471
25ARGARGDD10 - 46813 - 471
16ARGARGCC10 - 46813 - 471
26ARGARGDD10 - 46813 - 471

NCS ensembles :
ID
1
2
3
4
5
6

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Adenosylhomocysteinase / / S-adenosyl-L-homocysteine hydrolase / AdoHcyase


Mass: 51735.031 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (bacteria)
Gene: ahcY, sahH, PA0432 / Plasmid: pMCSG57 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): CodonPlus RILP / References: UniProt: Q9I685, adenosylhomocysteinase

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Non-polymers , 7 types, 1639 molecules

#2: Chemical
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: K
#3: Chemical
ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: PO4
#4: Chemical
ChemComp-NAD / NICOTINAMIDE-ADENINE-DINUCLEOTIDE / Nicotinamide adenine dinucleotide


Mass: 663.425 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C21H27N7O14P2 / Comment: NAD*YM
#5: Chemical
ChemComp-ADE / ADENINE / Adenine


Mass: 135.127 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C5H5N5
#6: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#7: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1616 / Source method: isolated from a natural source / Formula: H2O

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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: 2.25 Å3/Da / Density % sol: 45.31 %
Crystal growTemperature: 292 K / Method: vapor diffusion, hanging drop
Details: 50 mM KH2PO4, 20% (w/v) PEG8000, 2 mM 2'-deoxyadenosine

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.3 / Wavelength: 0.895 Å
DetectorType: RAYONIX MX-225 / Detector: CCD / Date: Dec 6, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.895 Å / Relative weight: 1
ReflectionResolution: 1.75→25 Å / Num. obs: 182928 / % possible obs: 99.9 % / Observed criterion σ(I): -3 / Redundancy: 4.2 % / Rmerge(I) obs: 0.078 / Net I/σ(I): 17.6
Reflection shellResolution: 1.75→1.81 Å

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Processing

Software
NameVersionClassification
REFMAC5.8.0155refinement
HKL-3000data reduction
HKL-3000data scaling
PHASERphasing
ARP/wARPmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6F3P
Resolution: 1.75→25 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.953 / SU B: 3.123 / SU ML: 0.054 / Cross valid method: THROUGHOUT / ESU R: 0.092 / ESU R Free: 0.088 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.16712 1806 1 %RANDOM
Rwork0.13976 ---
obs0.14003 181035 99.69 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 25.543 Å2
Baniso -1Baniso -2Baniso -3
1-0.03 Å2-0 Å2-0.08 Å2
2--0.24 Å20 Å2
3----0.22 Å2
Refinement stepCycle: 1 / Resolution: 1.75→25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14196 0 268 1616 16080
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.01914981
X-RAY DIFFRACTIONr_bond_other_d0.0020.0214411
X-RAY DIFFRACTIONr_angle_refined_deg1.6571.95520356
X-RAY DIFFRACTIONr_angle_other_deg0.983333226
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.35151915
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.56225.184652
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.988152648
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.4231572
X-RAY DIFFRACTIONr_chiral_restr0.1030.22284
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0217627
X-RAY DIFFRACTIONr_gen_planes_other0.0020.023285
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.0521.8497459
X-RAY DIFFRACTIONr_mcbond_other1.0521.8497458
X-RAY DIFFRACTIONr_mcangle_it1.4942.7719345
X-RAY DIFFRACTIONr_mcangle_other1.4942.7719346
X-RAY DIFFRACTIONr_scbond_it1.6312.0687522
X-RAY DIFFRACTIONr_scbond_other1.6312.0687522
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.5013.0310980
X-RAY DIFFRACTIONr_long_range_B_refined4.23523.67417424
X-RAY DIFFRACTIONr_long_range_B_other4.06622.9717011
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A306820.07
12B306820.07
21A307840.07
22C307840.07
31A309220.06
32D309220.06
41B305560.06
42C305560.06
51B306180.06
52D306180.06
61C307340.06
62D307340.06
LS refinement shellResolution: 1.753→1.798 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.196 133 -
Rwork0.177 13008 -
obs--97.39 %
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)
10.240.0344-0.15480.1715-0.02350.4893-0.02360.00360.00150.0345-0.0134-0.017-0.00440.09540.0370.012-0.0067-0.00870.0660.01840.07672.324616.189719.3771
20.0405-0.06830.10260.2402-0.05910.424-0.00720.00540.00160.04-0.001-0.0279-0.05150.02090.00810.0656-0.0203-0.01290.02130.00870.077554.217737.378127.8641
30.48660.0633-0.08110.0416-0.01860.0280.01240.0359-0.0149-0.0068-0.0225-0.01220.02240.0140.01010.05160.02320.01320.04750.00860.078457.43928.34817.175
40.1040.0587-0.07630.11950.06090.39030.00780.003-0.0098-0.0215-0.0144-0.0075-0.0249-0.03110.00650.0480.00710.00620.03340.00050.064724.910124.7478-8.632
50.481-0.0255-0.09510.16450.00010.0644-0.0330.0193-0.05720.0196-0.0030.0085-0.01020.00180.03610.0435-0.00230.01890.0261-0.00590.079127.29056.097413.8156
60.0980.05510.17640.09320.04660.3655-0.0140.01060.0061-0.0245-0.0152-0.0246-0.01730.02980.02920.0556-0.00170.0210.03660.00840.074744.06731.8854-1.8828
70.2146-0.3011-0.27150.54220.34960.4122-0.1343-0.03340.04420.25720.1383-0.05640.10710.0269-0.0040.19580.05-0.07210.05660.00010.035848.444626.613961.4907
80.41950.0515-0.06850.21890.02850.1185-0.0565-0.0167-0.01940.03780.0084-0.0150.01770.00310.04810.07190.0070.010.02270.01760.054146.10885.554341.5515
90.1544-0.20660.16860.4299-0.00760.4958-0.0874-0.01980.02870.16310.0153-0.0103-0.0201-0.03690.07210.12640.00810.00780.0066-0.01430.045630.405534.711655.3176
100.2507-0.09630.01050.04560.00570.28-0.0204-0.0097-0.00550.0002-0.0153-0.0074-0.0004-0.05810.03580.0326-0.00660.02240.0649-0.00960.05671.156718.813235.1661
110.0516-0.01230.1570.24540.04580.6254-0.0043-0.0104-0.0098-0.0058-0.0187-0.0069-0.0869-0.0470.02310.07340.01250.0070.0255-0.0090.063720.624238.359425.2553
120.5031-0.1134-0.08030.02690.01910.0231-0.0147-0.0369-0.00880.00450.0046-0.00460.0226-0.01460.01010.0791-0.01510.02870.0604-0.00080.054715.457811.214648.2088
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A10 - 205
2X-RAY DIFFRACTION2A206 - 381
3X-RAY DIFFRACTION3A382 - 469
4X-RAY DIFFRACTION4B10 - 194
5X-RAY DIFFRACTION5B195 - 381
6X-RAY DIFFRACTION6B382 - 469
7X-RAY DIFFRACTION7C10 - 205
8X-RAY DIFFRACTION8C206 - 381
9X-RAY DIFFRACTION9C382 - 469
10X-RAY DIFFRACTION10D9 - 205
11X-RAY DIFFRACTION11D206 - 381
12X-RAY DIFFRACTION12D382 - 469

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