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- PDB-2w01: Crystal structure of the guanylyl cyclase Cya2 -

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Basic information

Entry
Database: PDB / ID: 2w01
TitleCrystal structure of the guanylyl cyclase Cya2
ComponentsADENYLATE CYCLASE
KeywordsLYASE / GUANYLYL CYCLASE / CLASS III NUCLEOTIDYL CYCLASE
Function / homology
Function and homology information


cAMP biosynthetic process / adenylate cyclase activity / intracellular signal transduction / identical protein binding / membrane
Similarity search - Function
CHASE2 / CHASE2 domain / CHASE2 / Nucleotide cyclase, GGDEF domain / Adenylyl- / guanylyl cyclase, catalytic domain / Adenylyl cyclase class-3/4/guanylyl cyclase / Adenylate and Guanylate cyclase catalytic domain / Guanylate cyclase domain profile. / Nucleotide cyclase / Alpha-Beta Plaits ...CHASE2 / CHASE2 domain / CHASE2 / Nucleotide cyclase, GGDEF domain / Adenylyl- / guanylyl cyclase, catalytic domain / Adenylyl cyclase class-3/4/guanylyl cyclase / Adenylate and Guanylate cyclase catalytic domain / Guanylate cyclase domain profile. / Nucleotide cyclase / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesSYNECHOCYSTIS SP. (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.31 Å
AuthorsRauch, A. / Leipelt, M. / Russwurm, M. / Steegborn, C.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2008
Title: Crystal Structure of the Guanylyl Cyclase Cya2.
Authors: Rauch, A. / Leipelt, M. / Russwurm, M. / Steegborn, C.
History
DepositionAug 8, 2008Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 30, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ADENYLATE CYCLASE
B: ADENYLATE CYCLASE
C: ADENYLATE CYCLASE
D: ADENYLATE CYCLASE
E: ADENYLATE CYCLASE
F: ADENYLATE CYCLASE


Theoretical massNumber of molelcules
Total (without water)133,2606
Polymers133,2606
Non-polymers00
Water8,431468
1
A: ADENYLATE CYCLASE
B: ADENYLATE CYCLASE


Theoretical massNumber of molelcules
Total (without water)44,4202
Polymers44,4202
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3680 Å2
ΔGint-13.2 kcal/mol
Surface area20890 Å2
MethodPQS
2
C: ADENYLATE CYCLASE
D: ADENYLATE CYCLASE


Theoretical massNumber of molelcules
Total (without water)44,4202
Polymers44,4202
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4690 Å2
ΔGint-28.1 kcal/mol
Surface area20560 Å2
MethodPQS
3
E: ADENYLATE CYCLASE
F: ADENYLATE CYCLASE


Theoretical massNumber of molelcules
Total (without water)44,4202
Polymers44,4202
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3950 Å2
ΔGint-26.1 kcal/mol
Surface area20500 Å2
MethodPQS
Unit cell
Length a, b, c (Å)62.445, 84.090, 115.328
Angle α, β, γ (deg.)90.00, 97.40, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11B
21A
31D
41C
51F
61E

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ASPASPARGARG5BB438 - 45011 - 23
21ASPASPARGARG5AA438 - 45011 - 23
31ASPASPARGARG5DD438 - 45011 - 23
41ASPASPARGARG5CC438 - 45011 - 23
51ASPASPARGARG5FF438 - 45011 - 23
61ASPASPARGARG5EE438 - 45011 - 23
12PHEPHEGLUGLU6BB452 - 45725 - 30
22PHEPHEGLUGLU6AA452 - 45725 - 30
32PHEPHEGLUGLU6DD452 - 45725 - 30
42PHEPHEGLUGLU6CC452 - 45725 - 30
52PHEPHEGLUGLU6FF452 - 45725 - 30
62PHEPHEGLUGLU6EE452 - 45725 - 30
13VALVALPHEPHE5BB465 - 48938 - 62
23VALVALPHEPHE5AA465 - 48938 - 62
33VALVALPHEPHE5DD465 - 48938 - 62
43VALVALPHEPHE5CC465 - 48938 - 62
53VALVALPHEPHE5FF465 - 48938 - 62
63VALVALPHEPHE5EE465 - 48938 - 62
14GLYGLYPHEPHE5BB493 - 49866 - 71
24GLYGLYPHEPHE5AA493 - 49866 - 71
34GLYGLYPHEPHE5DD493 - 49866 - 71
44GLYGLYPHEPHE5CC493 - 49866 - 71
54GLYGLYPHEPHE5FF493 - 49866 - 71
64GLYGLYPHEPHE5EE493 - 49866 - 71
15GLYGLYSERSER6BB499 - 50372 - 76
25GLYGLYSERSER6AA499 - 50372 - 76
35GLYGLYSERSER6DD499 - 50372 - 76
45GLYGLYSERSER6CC499 - 50372 - 76
55GLYGLYSERSER6FF499 - 50372 - 76
65GLYGLYSERSER6EE499 - 50372 - 76
16LEULEUVALVAL6BB509 - 52582 - 98
26LEULEUVALVAL6AA509 - 52582 - 98
36LEULEUVALVAL6DD509 - 52582 - 98
46LEULEUVALVAL6CC509 - 52582 - 98
56LEULEUVALVAL6FF509 - 52582 - 98
66LEULEUVALVAL6EE509 - 52582 - 98
17LEULEUVALVAL6BB537 - 550110 - 123
27LEULEUVALVAL6AA537 - 550110 - 123
37LEULEUVALVAL6DD537 - 550110 - 123
47LEULEUVALVAL6CC537 - 550110 - 123
57LEULEUVALVAL6FF537 - 550110 - 123
67LEULEUVALVAL6EE537 - 550110 - 123
18VALVALTHRTHR5BB563 - 588136 - 161
28VALVALTHRTHR5AA563 - 588136 - 161
38VALVALTHRTHR5DD563 - 588136 - 161
48VALVALTHRTHR5CC563 - 588136 - 161
58VALVALTHRTHR5FF563 - 588136 - 161
68VALVALTHRTHR5EE563 - 588136 - 161
19THRTHRHISHIS6BB589 - 598162 - 171
29THRTHRHISHIS6AA589 - 598162 - 171
39THRTHRHISHIS6DD589 - 598162 - 171
49THRTHRHISHIS6CC589 - 598162 - 171
59THRTHRHISHIS6FF589 - 598162 - 171
69THRTHRHISHIS6EE589 - 598162 - 171
110ASPASPSERSER6BB618 - 629191 - 202
210ASPASPSERSER6AA618 - 629191 - 202
310ASPASPSERSER6DD618 - 629191 - 202
410ASPASPSERSER6CC618 - 629191 - 202
510ASPASPSERSER6FF618 - 629191 - 202
610ASPASPSERSER6EE618 - 629191 - 202

NCS oper:
IDCodeMatrixVector
1given(-0.8912, -0.2597, 0.3718), (-0.2561, -0.3884, -0.885), (0.3743, -0.8841, 0.2797)9.313, -65.27, -47.56
2given(0.9043, -0.06519, 0.4218), (0.2494, 0.8827, -0.3982), (-0.3464, 0.4653, 0.8145)46.4, -13.55, 32
3given(-0.9998, 0.000978, -0.02079), (0.01352, -0.7289, -0.6845), (-0.01582, -0.6847, 0.7287)-21.4, -100.2, -11.35
4given(0.9996, -0.02795, -0.001531), (-0.02132, -0.7249, -0.6885), (0.01813, 0.6883, -0.7252)-23.63, -72.43, -129.6
5given(-0.9005, 0.4232, -0.09958), (-0.2489, -0.3141, 0.9162), (0.3565, 0.8498, 0.3882)0.5378, 84.24, -30.05

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Components

#1: Protein
ADENYLATE CYCLASE / GUANYLYL CYCLASE CYA2


Mass: 22210.057 Da / Num. of mol.: 6 / Fragment: CATALYTIC DOMAIN, RESIDUES 434-635
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SYNECHOCYSTIS SP. (bacteria) / Strain: PCC 6803 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P72951, guanylate cyclase
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 468 / Source method: isolated from a natural source / Formula: H2O
Sequence details6 N-TERMINAL RESIDUES ARE CLONING ARTIFACT

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.29 Å3/Da / Density % sol: 45.79 % / Description: NONE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.99
DetectorType: MARRESEARCH / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.99 Å / Relative weight: 1
ReflectionResolution: 2.3→50 Å / Num. obs: 50776 / % possible obs: 97.3 % / Observed criterion σ(I): -3 / Redundancy: 3.6 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 8.4
Reflection shellResolution: 2.3→2.38 Å / Redundancy: 3 % / Rmerge(I) obs: 0.38 / % possible all: 85

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1WC1
Resolution: 2.31→19.94 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.894 / SU B: 17.65 / SU ML: 0.216 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.433 / ESU R Free: 0.296 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.282 2597 5.1 %RANDOM
Rwork0.194 ---
obs0.198 48079 97 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 41.44 Å2
Baniso -1Baniso -2Baniso -3
1--0.02 Å20 Å20.08 Å2
2--0.17 Å20 Å2
3----0.13 Å2
Refinement stepCycle: LAST / Resolution: 2.31→19.94 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8911 0 0 468 9379
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0190.0229037
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.9221.96412259
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.16951187
X-RAY DIFFRACTIONr_dihedral_angle_2_deg40.79624.974382
X-RAY DIFFRACTIONr_dihedral_angle_3_deg22.863151512
X-RAY DIFFRACTIONr_dihedral_angle_4_deg23.3841554
X-RAY DIFFRACTIONr_chiral_restr0.1480.21443
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.026780
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2530.24183
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.310.26054
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2040.2435
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2920.2142
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2430.216
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.9431.56007
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.59729416
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.43133377
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.8454.52843
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1B280medium positional0.190.5
2A280medium positional0.180.5
3D280medium positional0.210.5
4C280medium positional0.170.5
5F280medium positional0.270.5
6E280medium positional0.180.5
1B727loose positional0.635
2A727loose positional0.655
3D727loose positional0.645
4C727loose positional0.635
5F727loose positional0.715
6E727loose positional0.725
1B280medium thermal1.482
2A280medium thermal1.622
3D280medium thermal0.912
4C280medium thermal1.832
5F280medium thermal1.612
6E280medium thermal1.222
1B727loose thermal3.210
2A727loose thermal4.4910
3D727loose thermal3.0410
4C727loose thermal3.9210
5F727loose thermal4.4210
6E727loose thermal2.9710
LS refinement shellResolution: 2.31→2.37 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.36 164
Rwork0.232 2849
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)
12.9275-1.1565-1.32751.47230.84441.1159-0.0064-0.30060.05840.05280.04590.0167-0.04080.2285-0.0394-0.079-0.0238-0.0381-0.0473-0.0638-0.0979-16.418-15.493-54.842
22.15690.15960.28661.56960.69780.681-0.01010.05270.0789-0.0179-0.03760.08170.0056-0.04120.0477-0.0821-0.0298-0.0097-0.1061-0.0193-0.11468.113-6.206-55.103
33.3705-0.65930.58351.72450.1880.76770.00170.05290.1751-0.13810.0929-0.2870.0216-0.0412-0.0946-0.0483-0.00330.0066-0.15860.0192-0.0413-27.074-38.197-96.884
43.3571-0.20920.31860.8599-0.37781.6911-0.03610.09890.2202-0.0487-0.0638-0.0330.05240.06280.1-0.04850.0123-0.0204-0.184-0.0098-0.1059-2.982-31.828-90.181
51.9254-0.744-0.97031.0097-0.20063.41170.2714-0.49350.53290.0294-0.0450.0503-0.14240.3361-0.2264-0.0091-0.07560.04850.1664-0.15430.15187.1569.997-93.654
65.82020.5412.09021.74840.63011.95090.0501-0.6288-0.1011-0.1622-0.1596-0.15910.0489-0.22490.1095-0.03470.04850.0108-0.09940.1056-0.080331.2242.382-99.289
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1B435 - 631
2X-RAY DIFFRACTION2A435 - 635
3X-RAY DIFFRACTION3D434 - 632
4X-RAY DIFFRACTION4C434 - 633
5X-RAY DIFFRACTION5F435 - 631
6X-RAY DIFFRACTION6E434 - 632

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