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- PDB-2mhb: THE STRUCTURE OF HORSE METHAEMOGLOBIN AT 2.0 ANGSTROMS RESOLUTION -

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Basic information

Entry
Database: PDB / ID: 2mhb
TitleTHE STRUCTURE OF HORSE METHAEMOGLOBIN AT 2.0 ANGSTROMS RESOLUTION
Components
  • HEMOGLOBIN (AQUO MET) (ALPHA CHAIN)
  • HEMOGLOBIN (AQUO MET) (BETA CHAIN)
KeywordsOXYGEN TRANSPORT
Function / homology
Function and homology information


hemoglobin alpha binding / haptoglobin binding / haptoglobin-hemoglobin complex / organic acid binding / hemoglobin complex / hydrogen peroxide catabolic process / oxygen carrier activity / oxygen binding / peroxidase activity / blood microparticle ...hemoglobin alpha binding / haptoglobin binding / haptoglobin-hemoglobin complex / organic acid binding / hemoglobin complex / hydrogen peroxide catabolic process / oxygen carrier activity / oxygen binding / peroxidase activity / blood microparticle / iron ion binding / heme binding / metal ion binding
Similarity search - Function
Hemoglobin, pi / Hemoglobin, alpha-type / Hemoglobin, beta-type / Globin/Protoglobin / Globins / Globin domain profile. / Globin-like / Globin / Globin / Globin-like superfamily ...Hemoglobin, pi / Hemoglobin, alpha-type / Hemoglobin, beta-type / Globin/Protoglobin / Globins / Globin domain profile. / Globin-like / Globin / Globin / Globin-like superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
PROTOPORPHYRIN IX CONTAINING FE / Hemoglobin subunit alpha / Hemoglobin subunit beta
Similarity search - Component
Biological speciesEquus caballus (horse)
MethodX-RAY DIFFRACTION / Resolution: 2 Å
AuthorsLadner, R.C. / Heidner, E.G. / Perutz, M.F.
Citation
Journal: J.Mol.Biol. / Year: 1977
Title: The structure of horse methaemoglobin at 2-0 A resolution.
Authors: Ladner, R.C. / Heidner, E.J. / Perutz, M.F.
#1: Journal: Nature / Year: 1968
Title: Three-Dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Angstroms Resolution,the Atomic Model
Authors: Perutz, M.F. / Muirhead, H. / Cox, J.M. / Goaman, L.C.G.
#2: Journal: J.Mol.Biol. / Year: 1976
Title: A Correction to the Sequence of the Alpha Chains of Horse Haemoglobin
Authors: Ladner, R.C. / Air, G.M. / Fogg, J.H.
#3: Journal: Atlas of Macromolecular Structure on Microfiche / Year: 1976
#4: Journal: Atlas of Protein Sequence and Structure (Data Section)
Year: 1972
History
DepositionFeb 14, 1977Deposition site: BNL / Processing site: BNL
SupersessionApr 18, 1977ID: 1MHB
Revision 1.0Jan 20, 1983Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 28, 2012Group: Other

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HEMOGLOBIN (AQUO MET) (ALPHA CHAIN)
B: HEMOGLOBIN (AQUO MET) (BETA CHAIN)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,4044
Polymers31,1712
Non-polymers1,2332
Water362
1
A: HEMOGLOBIN (AQUO MET) (ALPHA CHAIN)
B: HEMOGLOBIN (AQUO MET) (BETA CHAIN)
hetero molecules

A: HEMOGLOBIN (AQUO MET) (ALPHA CHAIN)
B: HEMOGLOBIN (AQUO MET) (BETA CHAIN)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,8078
Polymers62,3414
Non-polymers2,4664
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Unit cell
Length a, b, c (Å)108.240, 63.130, 54.540
Angle α, β, γ (deg.)90.00, 110.85, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein HEMOGLOBIN (AQUO MET) (ALPHA CHAIN)


Mass: 15138.280 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Equus caballus (horse) / References: UniProt: P01958
#2: Protein HEMOGLOBIN (AQUO MET) (BETA CHAIN)


Mass: 16032.274 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Equus caballus (horse) / References: UniProt: P02062
#3: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.79 Å3/Da / Density % sol: 55.95 %
Crystal grow
*PLUS
Method: other / Details: Perutz, M.F., (1968) J. Crystal Growth, 2, 54.

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
Reflection
*PLUS
Num. obs: 23962

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Processing

RefinementRfactor Rwork: 0.23 / Rfactor obs: 0.23 / Highest resolution: 2 Å
Details: RESIDUES LYS A 61 AND LYS B 66 MAY FORM HYDROGEN BONDS TO THE PROPIONIC ACID SIDE CHAINS OF THEIR RESPECTIVE HEME GROUPS BUT THESE REGIONS ARE POORLY RESOLVED.
Refinement stepCycle: LAST / Highest resolution: 2 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2203 0 86 2 2291
Refinement
*PLUS
Rfactor obs: 0.231
Solvent computation
*PLUS
Displacement parameters
*PLUS

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