2hhd

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Revision as of 20:03, 7 February 2010

spinqualitylabelsall models PDB ID 2hhd Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
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, 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 with 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

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