2hhd: Difference between revisions

Revision as of 06:18, 18 February 2009

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2hhd.png

2hhd, resolution 2.20Å (default scene)

Ligands:

HEM, SO4

Structural annotation:
Resources:	CATH : 2Hhda00, 2Hhdb00, 2Hhdc00, 2Hhdd00 InterPro : Ipr002339, Ipr002338, Ipr000971, Ipr009050, Ipr002337, Ipr012292 Pfam : PF00042 SCOP : d2hhda_, d2hhdb_, d2hhdc_, d2hhdd_ UniProt : P69905, P68871

Functional annotation:
Cellular component:	hemoglobin complex
Biological process:	transport oxygen transport positive regulation of nitric oxide biosynthetic process nitric oxide transport regulation of blood vessel size regulation of blood pressure
Molecular function:	oxygen binding protein binding metal ion binding oxygen transporter activity heme binding iron ion binding hemoglobin binding selenium binding

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA-CHAINS IN HUMAN AND BOVINE HEMOGLOBIN

Template:ABSTRACT PUBMED 8639677

About this Structure

2HHD is a 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Pechik I, Ji X, Fidelis K, Karavitis M, Moult J, Brinigar WS, Fronticelli C, Gilliland GL. Crystallographic, molecular modeling, and biophysical characterization of the valine beta 67 (E11)-->threonine variant of hemoglobin. Biochemistry. 1996 Feb 13;35(6):1935-45. PMID:8639677 doi:10.1021/bi9519967

Page seeded by OCA on Wed Feb 18 08:18:03 2009

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Pechik I, Ji X, Fidelis K, Karavitis M, Moult J, Brinigar WS, Fronticelli C, Gilliland GL. Crystallographic, molecular modeling, and biophysical characterization of the valine beta 67 (E11)-->threonine variant of hemoglobin. Biochemistry. 1996 Feb 13;35(6):1935-45. PMID:8639677 doi:10.1021/bi9519967

@@ Line 20: / Line 20: @@
 ==About this Structure==
-HHD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HHD OCA].
+HHD is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HHD OCA].
 ==Reference==
-Crystallographic, molecular modeling, and biophysical characterization of the valine beta 67 (E11)--&gt;threonine variant of hemoglobin., Pechik I, Ji X, Fidelis K, Karavitis M, Moult J, Brinigar WS, Fronticelli C, Gilliland GL, Biochemistry. 1996 Feb 13;35(6):1935-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8639677 8639677]
+<ref group="xtra">PMID:8639677</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
 [[Category: Fronticelli, C.]]
 [[Category: Gilliland, G L.]]
@@ Line 32: / Line 31: @@
 [[Category: Oxygen transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat Jul  5 16:23:36 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:18:03 2009''

2hhd: Difference between revisions

Revision as of 06:18, 18 February 2009

OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA-CHAINS IN HUMAN AND BOVINE HEMOGLOBIN

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

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