2hhd

(Difference between revisions)

Revision as of 09:49, 11 March 2013

2hhd, resolution 2.20Å ()

Ligands:

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,

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

2hhd is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

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

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-[[Image:2hhd.png|left|200px]]
 {{STRUCTURE_2hhd|  PDB=2hhd  |  SCENE=  }}
 ===OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA-CHAINS IN HUMAN AND BOVINE HEMOGLOBIN===
 {{ABSTRACT_PUBMED_8639677}}