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- PDB-1xye: T-to-THigh Transitions in Human Hemoglobin: alpha Y42A deoxy low salt -

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Basic information

Entry
Database: PDB / ID: 1xye
TitleT-to-THigh Transitions in Human Hemoglobin: alpha Y42A deoxy low salt
Components
  • Hemoglobin alpha chain
  • Hemoglobin beta chain
KeywordsTRANSPORT PROTEIN / hemoglobin mutant / globin
Function / homology
Function and homology information


organic acid binding / nitric oxide transport / hemoglobin alpha binding / cellular oxidant detoxification / hemoglobin binding / haptoglobin-hemoglobin complex / renal absorption / hemoglobin complex / oxygen transport / Scavenging of heme from plasma ...organic acid binding / nitric oxide transport / hemoglobin alpha binding / cellular oxidant detoxification / hemoglobin binding / haptoglobin-hemoglobin complex / renal absorption / hemoglobin complex / oxygen transport / Scavenging of heme from plasma / endocytic vesicle lumen / blood vessel diameter maintenance / hydrogen peroxide catabolic process / oxygen carrier activity / carbon dioxide transport / response to hydrogen peroxide / Heme signaling / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / Late endosomal microautophagy / Cytoprotection by HMOX1 / oxygen binding / regulation of blood pressure / platelet aggregation / Chaperone Mediated Autophagy / positive regulation of nitric oxide biosynthetic process / tertiary granule lumen / Factors involved in megakaryocyte development and platelet production / blood microparticle / ficolin-1-rich granule lumen / iron ion binding / inflammatory response / heme binding / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / metal ion binding / membrane / cytosol
Similarity search - Function
Hemoglobin, pi / Hemoglobin, alpha-type / Hemoglobin, beta-type / : / Globin/Protoglobin / Globins / Globin-like / Globin / Globin / Globin domain profile. ...Hemoglobin, pi / Hemoglobin, alpha-type / Hemoglobin, beta-type / : / Globin/Protoglobin / Globins / Globin-like / Globin / Globin / Globin domain profile. / Globin-like superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
PROTOPORPHYRIN IX CONTAINING FE / Hemoglobin subunit alpha / Hemoglobin subunit beta / Hemoglobin subunit alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.13 Å
AuthorsKavanaugh, J.S. / Rogers, P.H. / Arnone, A. / Hui, H.L. / Wierzba, A. / DeYoung, A. / Kwiatkowski, L.D. / Noble, R.W. / Juszczak, L.J. / Peterson, E.S. / Friedman, J.M.
Citation
Journal: Biochemistry / Year: 2005
Title: Intersubunit interactions associated with tyr42alpha stabilize the quaternary-T tetramer but are not major quaternary constraints in deoxyhemoglobin
Authors: Kavanaugh, J.S. / Rogers, P.H. / Arnone, A. / Hui, H.L. / Wierzba, A. / Deyoung, A. / Kwiatkowski, L.D. / Noble, R.W. / Juszczak, L.J. / Peterson, E.S. / Friedman, J.M.
#1: Journal: To be Published
Title: Crystallographic Evidence for a New Ensemble of Ligand-Induced Allosteric Transitions in Hemoglobin: The T-to-THigh Quaternary Transitions
Authors: Kavanaugh, J.S. / Rogers, P.H. / Arnone, A.
History
DepositionNov 9, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 30, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 20, 2021Group: Database references / Derived calculations / Category: database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Aug 23, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Hemoglobin alpha chain
B: Hemoglobin beta chain
C: Hemoglobin alpha chain
D: Hemoglobin beta chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,4278
Polymers61,9614
Non-polymers2,4664
Water3,081171
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11140 Å2
ΔGint-106 kcal/mol
Surface area23840 Å2
MethodPISA
Unit cell
Length a, b, c (Å)97.000, 99.300, 66.200
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Detailsthe crystallographic asymmetric unit in this entry is an alpha2beta2 tetramer. the biological unit is an alpha2beta2 tetramer. The biological unit and crystallographic asymmetric unit are equivalent

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Components

#1: Protein Hemoglobin alpha chain


Mass: 15090.321 Da / Num. of mol.: 2 / Mutation: V1M, Y42A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HBA1 / Production host: Escherichia coli (E. coli) / References: UniProt: P01922, UniProt: P69905*PLUS
#2: Protein Hemoglobin beta chain


Mass: 15890.198 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Tissue: blood / References: UniProt: P68871
#3: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 171 / 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: 2.57 Å3/Da / Density % sol: 52.19 %
Crystal growTemperature: 298 K / Method: batch / pH: 7
Details: 10% PEG 6000, 10 mM potassium phosphate, 100 mM potassium chloride, 3 mM sodium dithionite, 10 mg/ml Hb, pH 7.0, batch, temperature 298K

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Data collection

DiffractionMean temperature: 298 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å
DetectorType: SDMS / Detector: AREA DETECTOR / Date: Nov 11, 1995 / Details: graphite
RadiationMonochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionHighest resolution: 2.13 Å / Num. all: 36379 / Num. obs: 36379 / % possible obs: 97.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.7 % / Rmerge(I) obs: 0.059 / Net I/σ(I): 5.4
Reflection shellResolution: 2.13→2.29 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.185 / Mean I/σ(I) obs: 1.3 / Num. unique all: 6440 / % possible all: 90.2

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Processing

Software
NameVersionClassification
REFMAC5refinement
SDMSdata reduction
SDMSdata scaling
X-PLORphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: pdb entry 1RQ3

1rq3


Resolution: 2.13→10 Å / Cor.coef. Fo:Fc: 0.942 / Cor.coef. Fo:Fc free: 0.904 / SU B: 9.493 / SU ML: 0.238 / Cross valid method: THROUGHOUT and Local R-free / σ(F): 0 / ESU R: 0.259 / ESU R Free: 0.207 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24126 3555 10.1 %10 mutually exclusive test sets matched to pdb entry 1RQ3
Rwork0.19156 ---
obs0.19655 31618 97.55 %-
all-31618 --
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: 19.671 Å2
Baniso -1Baniso -2Baniso -3
1--0.58 Å20 Å20 Å2
2--0.94 Å20 Å2
3----0.36 Å2
Refinement stepCycle: LAST / Resolution: 2.13→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4366 0 172 171 4709
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0210.0224708
X-RAY DIFFRACTIONr_bond_other_d0.0010.024168
X-RAY DIFFRACTIONr_angle_refined_deg1.9672.0576418
X-RAY DIFFRACTIONr_angle_other_deg1.18939674
X-RAY DIFFRACTIONr_dihedral_angle_1_deg3.9513570
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.82115755
X-RAY DIFFRACTIONr_chiral_restr0.1040.2698
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.025176
X-RAY DIFFRACTIONr_gen_planes_other0.0070.02886
X-RAY DIFFRACTIONr_nbd_refined0.2480.31145
X-RAY DIFFRACTIONr_nbd_other0.2070.33847
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2240.5195
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.1990.57
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1490.38
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2790.318
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1780.57
X-RAY DIFFRACTIONr_mcbond_it0.8041.52858
X-RAY DIFFRACTIONr_mcangle_it1.49224564
X-RAY DIFFRACTIONr_scbond_it2.51431850
X-RAY DIFFRACTIONr_scangle_it4.0124.51854
LS refinement shellResolution: 2.13→2.292 Å / Total num. of bins used: 7 /
RfactorNum. reflection
Rfree0.328 602
Rwork0.279 5703

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