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- PDB-2uum: Crystal structure of C-phycocyanin from Phormidium, Lyngbya spp. ... -

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Basic information

Entry
Database: PDB / ID: 2uum
TitleCrystal structure of C-phycocyanin from Phormidium, Lyngbya spp. (Marine) and Spirulina sp. (Fresh water) shows two different ways of energy transfer between two hexamers.
Components
  • (C-PHYCOCYANIN BETA ...) x 2
  • C-PHYCOCYANIN ALPHA CHAIN
KeywordsELECTRON TRANSPORT / PHOTOSYNTHESIS / SPIRULINA SP / C-PHYCOCYANIN / PHYCOBILISOME / MARINE / TRANSPORT / LYNGBYA SP / PHORMIDIUM / CHROMOPHORE / FRESH WATER / METHYLATION / BILE PIGMENT
Function / homology
Function and homology information


phycobilisome / plasma membrane-derived thylakoid membrane / photosynthesis
Similarity search - Function
Phycocyanin, alpha subunit / Phycocyanin, beta subunit / Phycocyanins / Phycobilisome, alpha/beta subunit / Phycobilisome, alpha/beta subunit superfamily / Phycobilisome protein / Globin-like / Globin-like superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
BILIVERDINE IX ALPHA / PHYCOCYANOBILIN / C-phycocyanin beta subunit / C-phycocyanin alpha subunit
Similarity search - Component
Biological speciesSPIRULINA SP. (bacteria)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsSatyanarayana, L. / Patel, A. / Mishra, S. / K Ghosh, P. / Suresh, C.G.
Citation
Journal: To be Published
Title: Crystal Structure of C-Phycocyanin from Phormidium, Lyngbya Spp. (Marine) and Spirulina Sp. (Fresh Water) Shows Two Different Ways of Energy Transfer between Two Hexamers.
Authors: Satyanarayana, L. / Patel, A. / Mishra, S. / Ghosh, P.K. / Suresh, C.G.
#1: Journal: To be Published
Title: Crystal Structure of C-Phycocyanin from Phormidium, Lyngbya Spp. (Marine) and Spirulina Sp. (Fresh Water) Shows Two Different Ways of Energy Transfer between Twohexamers.
Authors: Satyanarayana, L. / Patel, A. / Mishra, S. / Ghosh, P.K. / Suresh, C.G.
History
DepositionMar 4, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 27, 2008Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 13, 2023Group: Data collection / Database references ...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 / 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 / _struct_conn.pdbx_leaving_atom_flag / _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
Revision 1.4Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: C-PHYCOCYANIN ALPHA CHAIN
B: C-PHYCOCYANIN BETA CHAIN
C: C-PHYCOCYANIN ALPHA CHAIN
D: C-PHYCOCYANIN BETA CHAIN
E: C-PHYCOCYANIN ALPHA CHAIN
F: C-PHYCOCYANIN BETA CHAIN
G: C-PHYCOCYANIN ALPHA CHAIN
H: C-PHYCOCYANIN BETA CHAIN
I: C-PHYCOCYANIN ALPHA CHAIN
J: C-PHYCOCYANIN BETA CHAIN
K: C-PHYCOCYANIN ALPHA CHAIN
L: C-PHYCOCYANIN BETA CHAIN
M: C-PHYCOCYANIN ALPHA CHAIN
N: C-PHYCOCYANIN BETA CHAIN
O: C-PHYCOCYANIN ALPHA CHAIN
P: C-PHYCOCYANIN BETA CHAIN
Q: C-PHYCOCYANIN ALPHA CHAIN
R: C-PHYCOCYANIN BETA CHAIN
S: C-PHYCOCYANIN ALPHA CHAIN
T: C-PHYCOCYANIN BETA CHAIN
U: C-PHYCOCYANIN ALPHA CHAIN
V: C-PHYCOCYANIN BETA CHAIN
W: C-PHYCOCYANIN ALPHA CHAIN
X: C-PHYCOCYANIN BETA CHAIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)449,32060
Polymers428,27224
Non-polymers21,04836
Water2,936163
1
A: C-PHYCOCYANIN ALPHA CHAIN
B: C-PHYCOCYANIN BETA CHAIN
C: C-PHYCOCYANIN ALPHA CHAIN
D: C-PHYCOCYANIN BETA CHAIN
E: C-PHYCOCYANIN ALPHA CHAIN
F: C-PHYCOCYANIN BETA CHAIN
G: C-PHYCOCYANIN ALPHA CHAIN
H: C-PHYCOCYANIN BETA CHAIN
I: C-PHYCOCYANIN ALPHA CHAIN
J: C-PHYCOCYANIN BETA CHAIN
K: C-PHYCOCYANIN ALPHA CHAIN
L: C-PHYCOCYANIN BETA CHAIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)224,61830
Polymers214,10012
Non-polymers10,51818
Water1448
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area33610 Å2
ΔGint-602.5 kcal/mol
Surface area95260 Å2
MethodPQS
2
M: C-PHYCOCYANIN ALPHA CHAIN
N: C-PHYCOCYANIN BETA CHAIN
O: C-PHYCOCYANIN ALPHA CHAIN
P: C-PHYCOCYANIN BETA CHAIN
Q: C-PHYCOCYANIN ALPHA CHAIN
R: C-PHYCOCYANIN BETA CHAIN
S: C-PHYCOCYANIN ALPHA CHAIN
T: C-PHYCOCYANIN BETA CHAIN
U: C-PHYCOCYANIN ALPHA CHAIN
V: C-PHYCOCYANIN BETA CHAIN
W: C-PHYCOCYANIN ALPHA CHAIN
X: C-PHYCOCYANIN BETA CHAIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)224,70230
Polymers214,17212
Non-polymers10,53018
Water1629
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area39090 Å2
ΔGint-340.6 kcal/mol
Surface area103560 Å2
MethodPQS
Unit cell
Length a, b, c (Å)107.332, 115.639, 183.258
Angle α, β, γ (deg.)90.00, 90.03, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
31E
41G
51I
61K
71M
81O
91Q
101S
111U
121W
12B
22D
32F
42H
52J
62L
72N
82P
92R
102T
112V
122X

NCS domain segments:

Component-ID: 1 / Beg auth comp-ID: MET / Beg label comp-ID: MET / End auth comp-ID: SER / End label comp-ID: SER / Refine code: 1

Dom-IDEns-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11AA1 - 1621 - 162
21CC1 - 1621 - 162
31EE1 - 1621 - 162
41GG1 - 1621 - 162
51II1 - 1621 - 162
61KK1 - 1621 - 162
71MM1 - 1621 - 162
81OO1 - 1621 - 162
91QQ1 - 1621 - 162
101SS1 - 1621 - 162
111UU1 - 1621 - 162
121WW1 - 1621 - 162
12BB1 - 1721 - 172
22DD1 - 1721 - 172
32FF1 - 1721 - 172
42HH1 - 1721 - 172
52JJ1 - 1721 - 172
62LL1 - 1721 - 172
72NN1 - 1721 - 172
82PP1 - 1721 - 172
92RR1 - 1721 - 172
102TT1 - 1721 - 172
112VV1 - 1721 - 172
122XX1 - 1721 - 172

NCS ensembles :
ID
1
2

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Components

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Protein , 1 types, 12 molecules ACEGIKMOQSUW

#1: Protein
C-PHYCOCYANIN ALPHA CHAIN


Mass: 17602.820 Da / Num. of mol.: 12 / Source method: isolated from a natural source
Details: PHYCOCYANOBILIN ATTACHED ALFA-84 CYSTIENE RESIDUE AND BETA-82 AND 153 MONOMERS
Source: (natural) SPIRULINA SP. (bacteria) / References: UniProt: P72509

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C-PHYCOCYANIN BETA ... , 2 types, 12 molecules BDFHJLNPRTVX

#2: Protein
C-PHYCOCYANIN BETA CHAIN


Mass: 18080.496 Da / Num. of mol.: 11 / Source method: isolated from a natural source
Details: PHYCOCYANOBILIN ATTACHED ALFA-84 CYSTIENE RESIDUE AND BETA-82 AND 153 MONOMERS.
Source: (natural) SPIRULINA SP. (bacteria) / References: UniProt: P72508
#3: Protein C-PHYCOCYANIN BETA CHAIN


Mass: 18152.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: PHYCOCYANOBILIN ATTACHED ALFA-84 CYSTIENE RESIDUE AND BETA-82 AND 153 MONOMERS.
Source: (natural) SPIRULINA SP. (bacteria) / References: UniProt: P72508

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Non-polymers , 3 types, 199 molecules

#4: Chemical
ChemComp-CYC / PHYCOCYANOBILIN


Mass: 588.694 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C33H40N4O6
#5: Chemical...
ChemComp-BLA / BILIVERDINE IX ALPHA


Mass: 582.646 Da / Num. of mol.: 24 / Source method: obtained synthetically / Formula: C33H34N4O6
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 163 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY
Sequence detailsTHE SPECIES FROM WHICH THE PROTEIN HAS BEEN EXTRACTED IS CURRENTLY UNKNOWN. IN THE PDB ENTRY IT HAS ...THE SPECIES FROM WHICH THE PROTEIN HAS BEEN EXTRACTED IS CURRENTLY UNKNOWN. IN THE PDB ENTRY IT HAS BEEN MATCHED TO SPIRULINA PLATENSIS WHICH HAS A SEQUENCE IDENTITY OF 98.14% (162 AMINO ACIDS) AND 97.674% (172 AMINO ACID CHAINS) AND HAS THE SAME GRANDPARENT IN THE TAXONOMY TREE.

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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: 2.5 Å3/Da / Density % sol: 50.6 % / Description: NONE
Crystal growpH: 6.5
Details: 0.01M SODIUM PHOSPHATE PH 6.5, 0.72 M SOD. FORMATE, AND 13.5% PEG 4K

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Data collection

DiffractionMean temperature: 110 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418
DetectorType: RIGAKU IMAGE PLATE / Detector: IMAGE PLATE / Details: MIRRORS
RadiationMonochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 3→40 Å / Num. obs: 86909 / % possible obs: 96.6 % / Observed criterion σ(I): 10 / Redundancy: 3 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 9.19
Reflection shellResolution: 3→3.11 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.02 / Mean I/σ(I) obs: 3.9 / % possible all: 93.8

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1GH0
Resolution: 3→182.57 Å / Cor.coef. Fo:Fc: 0.914 / Cor.coef. Fo:Fc free: 0.867 / SU B: 17.981 / SU ML: 0.333 / Cross valid method: THROUGHOUT / ESU R Free: 0.463 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.242 4331 5 %RANDOM
Rwork0.201 ---
obs0.203 82635 96.5 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 25.03 Å2
Baniso -1Baniso -2Baniso -3
1--0.46 Å20 Å20.13 Å2
2--4.08 Å20 Å2
3----3.63 Å2
Refinement stepCycle: LAST / Resolution: 3→182.57 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms29897 0 1548 163 31608
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.02232003
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg2.3782.02343552
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.53753984
X-RAY DIFFRACTIONr_dihedral_angle_2_deg39.31524.0951260
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.192154912
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.01815204
X-RAY DIFFRACTIONr_chiral_restr0.1210.24813
X-RAY DIFFRACTIONr_gen_planes_refined0.010.0224392
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2710.217031
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.320.222961
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1420.21027
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.4750.2177
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.3480.212
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.6451.520171
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.117231571
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.367324685
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.1544.511981
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

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A1229tight positional0.080.05
12C1229tight positional0.090.05
13E1229tight positional0.080.05
14G1229tight positional0.080.05
15I1229tight positional0.080.05
16K1229tight positional0.090.05
17M1229tight positional0.090.05
18O1229tight positional0.090.05
19Q1229tight positional0.080.05
110S1229tight positional0.080.05
111U1229tight positional0.080.05
112W1229tight positional0.080.05
21B1254tight positional0.070.05
22D1254tight positional0.090.05
23F1254tight positional0.080.05
24H1254tight positional0.090.05
25J1254tight positional0.090.05
26L1254tight positional0.070.05
27N1254tight positional0.080.05
28P1254tight positional0.080.05
29R1254tight positional0.080.05
210T1254tight positional0.070.05
211V1254tight positional0.090.05
212X1254tight positional0.080.05
11A1229tight thermal0.160.5
12C1229tight thermal0.150.5
13E1229tight thermal0.150.5
14G1229tight thermal0.150.5
15I1229tight thermal0.160.5
16K1229tight thermal0.140.5
17M1229tight thermal0.170.5
18O1229tight thermal0.150.5
19Q1229tight thermal0.150.5
110S1229tight thermal0.150.5
111U1229tight thermal0.150.5
112W1229tight thermal0.150.5
21B1254tight thermal0.140.5
22D1254tight thermal0.150.5
23F1254tight thermal0.140.5
24H1254tight thermal0.150.5
25J1254tight thermal0.150.5
26L1254tight thermal0.150.5
27N1254tight thermal0.150.5
28P1254tight thermal0.140.5
29R1254tight thermal0.150.5
210T1254tight thermal0.150.5
211V1254tight thermal0.150.5
212X1254tight thermal0.160.5
LS refinement shellResolution: 3→3.08 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.313 321
Rwork0.256 5834

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