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PDBsum entry 2mhb

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protein ligands Protein-protein interface(s) links
Oxygen transport PDB id
2mhb
Jmol
Contents
Protein chains
141 a.a. *
146 a.a. *
Ligands
HEM ×2
Waters ×2
* Residue conservation analysis
PDB id:
2mhb
Name: Oxygen transport
Title: The structure of horse methaemoglobin at 2.0 angstroms resol
Structure: Hemoglobin (aquo met) (alpha chain). Chain: a. Engineered: yes. Hemoglobin (aquo met) (beta chain). Chain: b. Engineered: yes
Source: Equus caballus. Horse. Organism_taxid: 9796. Organism_taxid: 9796
Biol. unit: Tetramer (from PQS)
Resolution:
2.00Å     R-factor:   0.230    
Authors: R.C.Ladner,E.G.Heidner,M.F.Perutz
Key ref:
R.C.Ladner et al. (1977). The structure of horse methaemoglobin at 2-0 A resolution. J Mol Biol, 114, 385-414. PubMed id: 561852 DOI: 10.1016/0022-2836(77)90256-X
Date:
14-Feb-77     Release date:   20-Jan-83    
Supersedes: 1mhb
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01958  (HBA_HORSE) -  Hemoglobin subunit alpha
Seq:
Struc:
142 a.a.
141 a.a.*
Protein chain
Pfam   ArchSchema ?
P02062  (HBB_HORSE) -  Hemoglobin subunit beta
Seq:
Struc:
146 a.a.
146 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     hemoglobin complex   1 term 
  Biological process     transport   2 terms 
  Biochemical function     oxygen binding     5 terms  

 

 
DOI no: 10.1016/0022-2836(77)90256-X J Mol Biol 114:385-414 (1977)
PubMed id: 561852  
 
 
The structure of horse methaemoglobin at 2-0 A resolution.
R.C.Ladner, E.J.Heidner, M.F.Perutz.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 16.
FIG 16. Hydrogen-bonding between helices Gq and G/3,.
Figure 17.
FIG. 17. Hydrogen-bonding at the c& contact near the centre of the molecule. Water molecules 18, 22 and 25 are common to Figues 16 and 17.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1977, 114, 385-414) copyright 1977.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
16782791 P.J.Kundrotas, and E.Alexov (2006).
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Optical absorption of tetraphenylporphyrin thin films in UV-vis-NIR region.
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15887226 R.Sankaranarayanan, B.K.Biswal, and M.Vijayan (2005).
A new relaxed state in horse methemoglobin characterized by crystallographic studies.
  Proteins, 60, 547-551.
PDB codes: 1y8h 1y8i 1y8k
11909691 M.Comporti, C.Signorini, G.Buonocore, and L.Ciccoli (2002).
Iron release, oxidative stress and erythrocyte ageing.
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12454461 M.K.Safo, J.C.Burnett, F.N.Musayev, S.Nokuri, and D.J.Abraham (2002).
Structure of human carbonmonoxyhemoglobin at 2.16 A: a snapshot of the allosteric transition.
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PDB code: 1ljw
11468400 A.Riccio, L.Vitagliano, G.di Prisco, A.Zagari, and L.Mazzarella (2001).
Liganded and unliganded forms of Antarctic fish haemoglobins in polyethylene glycol: crystallization of an R-state haemichrome intermediate.
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11151007 J.C.Burnett, P.Botti, D.J.Abraham, and G.E.Kellogg (2001).
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11369847 M.K.Safo, and D.J.Abraham (2001).
The X-ray structure determination of bovine carbonmonoxy hemoglobin at 2.1 A resoultion and its relationship to the quaternary structures of other hemoglobin crystal froms.
  Protein Sci, 10, 1091-1099.
PDB code: 1fsx
11375496 X.Z.Liu, S.L.Li, H.Jing, Y.H.Liang, Z.Q.Hua, and G.Y.Lu (2001).
Avian haemoglobins and structural basis of high affinity for oxygen: structure of bar-headed goose aquomet haemoglobin.
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PDB code: 1c40
11112521 T.C.Mueser, P.H.Rogers, and A.Arnone (2000).
Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin.
  Biochemistry, 39, 15353-15364.
PDB codes: 1g08 1g09 1g0a 1g0b
10713517 T.H.Lu, K.Panneerselvam, Y.C.Liaw, P.Kan, and C.J.Lee (2000).
Structure determination of porcine haemoglobin.
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PDB code: 1qpw
10037733 J.E.Knapp, M.A.Oliveira, Q.Xie, S.R.Ernst, A.F.Riggs, and M.L.Hackert (1999).
The structural and functional analysis of the hemoglobin D component from chicken.
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PDB code: 1hbr
10500299 J.R.Tame (1999).
What is the true structure of liganded haemoglobin?
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10096879 N.Ramadas, and J.M.Rifkind (1999).
Molecular dynamics of human methemoglobin: the transmission of conformational information between subunits in an alpha beta dimer.
  Biophys J, 76, 1796-1811.  
10328266 S.M.King, and W.C.Johnson (1999).
Assigning secondary structure from protein coordinate data.
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9761903 G.B.Vásquez, X.Ji, C.Fronticelli, and G.L.Gilliland (1998).
Human carboxyhemoglobin at 2.2 A resolution: structure and solvent comparisons of R-state, R2-state and T-state hemoglobins.
  Acta Crystallogr D Biol Crystallogr, 54, 355-366.
PDB code: 1aj9
9188741 A.V.Efimov (1997).
Structural trees for protein superfamilies.
  Proteins, 28, 241-260.  
9199803 E.Balog, K.Kis-Petik, J.Fidy, M.Köhler, and J.Friedrich (1997).
Interpretation of multiple Q(0,0) bands in the absorption spectrum of Mg-mesoporphyrin embedded in horseradish peroxidase.
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9032082 K.S.Kroeger, and C.E.Kundrot (1997).
Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins.
  Structure, 5, 227-237.
PDB codes: 1abw 1aby
8756522 I.A.Vakser (1996).
Low-resolution docking: prediction of complexes for underdetermined structures.
  Biopolymers, 39, 455-464.  
8639677 I.Pechik, X.Ji, K.Fidelis, M.Karavitis, J.Moult, W.S.Brinigar, C.Fronticelli, and G.L.Gilliland (1996).
Crystallographic, molecular modeling, and biophysical characterization of the valine beta 67 (E11)-->threonine variant of hemoglobin.
  Biochemistry, 35, 1935-1945.
PDB codes: 1hdb 2hhd
8755735 K.R.Rodgers, G.S.Lukat-Rodgers, and J.A.Barron (1996).
Structural basis for ligand discrimination and response initiation in the heme-based oxygen sensor FixL.
  Biochemistry, 35, 9539-9548.  
8631366 M.Coletta, M.Angeletti, G.De Sanctis, L.Cerroni, B.Giardina, G.Amiconi, and P.Ascenzi (1996).
Kinetic evidence for the existence of a rate-limiting step in the reaction of ferric hemoproteins with anionic ligands.
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7669916 J.C.Hempel, R.M.Fine, M.Hassan, W.Ghoul, A.Guaragna, S.C.Koerber, Z.Li, and A.T.Hagler (1995).
Conformational analysis of endothelin-1: effects of solvation free energy.
  Biopolymers, 36, 283-301.  
7829496 M.Nagai, S.Kaminaka, Y.Ohba, Y.Nagai, Y.Mizutani, and T.Kitagawa (1995).
Ultraviolet resonance Raman studies of quaternary structure of hemoglobin using a tryptophan beta 37 mutant.
  J Biol Chem, 270, 1636-1642.  
7731951 I.A.Vakser, and C.Aflalo (1994).
Hydrophobic docking: a proposed enhancement to molecular recognition techniques.
  Proteins, 20, 320-329.  
8471730 A.Ansari, C.M.Jones, E.R.Henry, J.Hofrichter, and W.A.Eaton (1993).
Photoselection in polarized photolysis experiments on heme proteins.
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8433384 J.Otsuka, K.Miyazaki, and K.Horimoto (1993).
Divergence pattern and selective mode in protein evolution: the example of vertebrate myoglobins and hemoglobin chains.
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1515540 D.L.Weaver (1992).
Hydrophobic interaction between globin helices.
  Biopolymers, 32, 477-490.  
1518802 D.L.Weaver (1992).
Modeling microdomains: the surface area of globin helices.
  Proteins, 13, 327-335.  
1549581 E.Katchalski-Katzir, I.Shariv, M.Eisenstein, A.A.Friesem, C.Aflalo, and I.A.Vakser (1992).
Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniques.
  Proc Natl Acad Sci U S A, 89, 2195-2199.  
1420989 M.L.Connolly (1992).
Shape distributions of protein topography.
  Biopolymers, 32, 1215-1236.  
1907667 J.Rose, and F.Eisenmenger (1991).
A fast unbiased comparison of protein structures by means of the Needleman-Wunsch algorithm.
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10044644 S.L.Chang, H.E.King, M.T.Huang, and Y.Gao (1991).
Direct phase determination of large macromolecular crystals using three-beam x-ray interference.
  Phys Rev Lett, 67, 3113-3116.  
2124278 K.Horimoto, H.Suzuki, and J.Otsuka (1990).
Discrimination between adaptive and neutral amino acid substitutions in vertebrate hemoglobins.
  J Mol Evol, 31, 302-324.  
2854395 D.L.Rousseau, M.Sassaroli, Y.C.Ching, and S.Dasgupta (1988).
The role of water near cytochrome a in cytochrome c oxidase.
  Ann N Y Acad Sci, 550, 223-237.  
3741993 M.L.Connolly (1986).
Shape complementarity at the hemoglobin alpha 1 beta 1 subunit interface.
  Biopolymers, 25, 1229-1247.  
3464965 R.B.Honzatko, and W.A.Hendrickson (1986).
Molecular models for the putative dimer of sea lamprey hemoglobin.
  Proc Natl Acad Sci U S A, 83, 8487-8491.  
3898068 R.Varadarajan, A.Szabo, and S.G.Boxer (1985).
Cloning, expression in Escherichia coli, and reconstitution of human myoglobin.
  Proc Natl Acad Sci U S A, 82, 5681-5684.  
6285999 J.P.Allen, J.T.Colvin, D.G.Stinson, C.P.Flynn, and H.J.Stapleton (1982).
Protein conformation from electron spin relaxation data.
  Biophys J, 38, 299-310.  
6171809 J.B.Clegg, and J.Gagnon (1981).
Structure of the zeta chain of human embryonic hemoglobin.
  Proc Natl Acad Sci U S A, 78, 6076-6080.  
7304605 W.F.Moo-Penn, P.McPhedran, S.Bobrow, M.H.Johnson, D.L.Jue, and K.W.Olsen (1981).
Hemoglobin connecticut (beta 21 (B3) Asp leads to Gly): a hemoglobin variant with low oxygen affinity.
  Am J Hematol, 11, 137-145.  
7380012 A.Bracht, B.R.Eufinger, H.J.Neumann, G.Niephaus, A.Redhardt, and J.Schlitter (1980).
Thermal fluctuations of large amplitude in the tertiary structure of methemoglobin.
  FEBS Lett, 114, 157-160.  
7379791 G.G.Van Beek, and S.H.De Bruin (1980).
Identification of the residues involved in the oxygen-linked chloride-ion binding sites in human deoxyhemoglobin and oxyhemoglobin.
  Eur J Biochem, 105, 353-360.  
7248452 G.K.Ackers (1980).
Energetics of subunit assembly and ligand binding in human hemoglobin.
  Biophys J, 32, 331-346.  
6932026 J.Greer (1980).
Model for haptoglobin heavy chain based upon structural homology.
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7248446 S.C.Harrison (1980).
Protein interfaces and intersubunit bonding. The case of tomato bushy stunt virus.
  Biophys J, 32, 139-153.  
233575 A.S.Brill, and D.A.Hampton (1979).
Quantitative evaluation of contributions to electron paramagnetic resonance line widths in ferric hemoglobin single crystals.
  Biophys J, 25, 313-322.  
233574 D.A.Hampton, and A.S.Brill (1979).
Crystalline state disorder and hyperfine component line widths in ferric hemoglobin chains.
  Biophys J, 25, 301-311.  
291973 J.A.Shelnutt, D.L.Rousseau, J.M.Friedman, and S.R.Simon (1979).
Protein-heme interaction in hemoglobin: evidence from Raman difference spectroscopy.
  Proc Natl Acad Sci U S A, 76, 4409-4413.  
220604 J.S.Valentine, R.P.Sheridan, L.C.Allen, and P.C.Kahn (1979).
Coupling between oxidation state and hydrogen bond conformation in heme proteins.
  Proc Natl Acad Sci U S A, 76, 1009-1013.  
399003 M.H.Klapper, and M.Faraggi (1979).
Applications of pulse radiolysis to protein chemistry.
  Q Rev Biophys, 12, 465-519.  
32039 G.G.Van Beek, E.R.Zuiderweg, and S.H.De Bruin (1978).
The binding of protons and inositol hexakisphosphate to ligated and unligated human des-Arg141alpha-hemoglobin.
  Eur J Biochem, 92, 309-316.  
656541 G.H.Loew, and R.F.Kirchner (1978).
Semiempirical calculations of model deoxyheme. Variation of calculated electromagnetic properties with electronic configuration and distance of iron from the plane.
  Biophys J, 22, 179-189.  
272646 J.Greer, and B.L.Bush (1978).
Macromolecular shape and surface maps by solvent exclusion.
  Proc Natl Acad Sci U S A, 75, 303-307.  
274697 P.W.Tucker, S.E.Phillips, M.F.Perutz, R.Houtchens, and W.S.Caughey (1978).
Structure of hemoglobins Zürich [His E7(63)beta replaced by Arg] and Sydney [Val E11(67)beta replaced by Ala] and role of the distal residues in ligand binding.
  Proc Natl Acad Sci U S A, 75, 1076-1080.  
283394 W.S.Bennett, and T.A.Steitz (1978).
Glucose-induced conformational change in yeast hexokinase.
  Proc Natl Acad Sci U S A, 75, 4848-4852.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.