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2NRM
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BU of 2nrm by Molmil
S-nitrosylated blackfin tuna myoglobin
Descriptor: GLYCEROL, Myoglobin, PROTOPORPHYRIN IX CONTAINING FE
Authors:Schreiter, E.R, Rodr guez, M.M, Weichsel, A, Montfort, W.R, Bonaventura, J.
Deposit date:2006-11-02
Release date:2007-05-08
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (1.09 Å)
Cite:S-nitrosylation-induced conformational change in blackfin tuna myoglobin.
J.Biol.Chem., 282, 2007
2NRL
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BU of 2nrl by Molmil
Blackfin tuna myoglobin
Descriptor: 1,2-ETHANEDIOL, Myoglobin, PROTOPORPHYRIN IX CONTAINING FE
Authors:Schreiter, E.R, Rodr guez, M.M, Weichsel, A, Montfort, W.R, Bonaventura, J.
Deposit date:2006-11-02
Release date:2007-05-08
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (0.91 Å)
Cite:S-nitrosylation-induced conformational change in blackfin tuna myoglobin.
J.Biol.Chem., 282, 2007
2NX0
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BU of 2nx0 by Molmil
Ferrous nitrosyl blackfin tuna myoglobin
Descriptor: Myoglobin, NITRIC OXIDE, PROTOPORPHYRIN IX CONTAINING FE, ...
Authors:Schreiter, E.R, Rodriguez, M.M, Weichsel, A, Montfort, W.R, Bonaventura, J.
Deposit date:2006-11-16
Release date:2007-05-08
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (0.95 Å)
Cite:S-nitrosylation-induced conformational change in blackfin tuna myoglobin.
J.Biol.Chem., 282, 2007
1SPG
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BU of 1spg by Molmil
CARBONMONOXY HEMOGLOBIN FROM THE TELEOST FISH LEIOSTOMUS XANTHURUS
Descriptor: CARBON MONOXIDE, HEMOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE
Authors:Mylvaganam, S.E, Getzoff, E.D.
Deposit date:1996-02-05
Release date:1997-03-12
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (1.95 Å)
Cite:Structural basis for the root effect in haemoglobin.
Nat.Struct.Biol., 3, 1996
1LLA
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BU of 1lla by Molmil
CRYSTAL STRUCTURE OF DEOXYGENATED LIMULUS POLYPHEMUS SUBUNIT II HEMOCYANIN AT 2.18 ANGSTROMS RESOLUTION: CLUES FOR A MECHANISM FOR ALLOSTERIC REGULATION
Descriptor: CHLORIDE ION, COPPER (II) ION, HEMOCYANIN (SUBUNIT TYPE II), ...
Authors:Hazes, B, Hol, W.G.J.
Deposit date:1992-09-07
Release date:1994-01-31
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.18 Å)
Cite:Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 A resolution: clues for a mechanism for allosteric regulation.
Protein Sci., 2, 1993
1HLB
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BU of 1hlb by Molmil
Structural analysis of monomeric hemichrome and dimeric cyanomet hemoglobins from Caudina arenicola
Descriptor: HEMOGLOBIN (DEOXY), PROTOPORPHYRIN IX CONTAINING FE
Authors:Hackert, M.L, Mitchell, D.T.
Deposit date:1994-03-22
Release date:1994-06-22
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Structural analysis of monomeric hemichrome and dimeric cyanomet hemoglobins from Caudina arenicola.
J.Mol.Biol., 251, 1995
1NOL
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BU of 1nol by Molmil
OXYGENATED HEMOCYANIN (SUBUNIT TYPE II)
Descriptor: CALCIUM ION, COPPER (II) ION, HEMOCYANIN (SUBUNIT TYPE II), ...
Authors:Hazes, B, Hol, W.G.J.
Deposit date:1995-10-17
Release date:1996-03-08
Last modified:2018-04-18
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 A resolution: clues for a mechanism for allosteric regulation.
Protein Sci., 2, 1993
1OXY
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BU of 1oxy by Molmil
CRYSTALLOGRAPHIC ANALYSIS OF OXYGENATED AND DEOXYGENATED STATES OF ARTHROPOD HEMOCYANIN SHOWS UNUSUAL DIFFERENCES
Descriptor: COPPER (II) ION, HEMOCYANIN (SUBUNIT TYPE II), OXYGEN MOLECULE
Authors:Ton-that, H, Magnus, K.
Deposit date:1995-01-06
Release date:1995-02-27
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences.
Proteins, 19, 1994
3NQS
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BU of 3nqs by Molmil
Crystal Structure of Inducible Nitric Oxide Synthase with N-Nitrosated-pterin
Descriptor: 1,2-ETHANEDIOL, 5,6,7,8-TETRAHYDROBIOPTERIN, ETHYL 4-[(4-METHYLPYRIDIN-2-YL)AMINO]PIPERIDINE-1-CARBOXYLATE, ...
Authors:Rosenfeld, R.J, Getzoff, E.D, Tainer, J.A.
Deposit date:2010-06-29
Release date:2010-07-21
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Nitric-oxide synthase forms N-NO-pterin and S-NO-cys: implications for activity, allostery, and regulation.
J.Biol.Chem., 285, 2010

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