1lqb | pdb_00001lqb

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File:1lqb.png

1lqb, resolution 2.00Å (default scene)

Ligands:

SO4

Non-Standard Residues:

HYP

Structural annotation:
Resources:	CATH : 1Lqba00, 1Lqbb00, 1Lqbc01, 1Lqbc02 InterPro : Ipr000626, Ipr001232, Ipr011333, Ipr002714, Ipr011598, Ipr013655, Ipr000014, Ipr000700, Ipr001610, Ipr001321, Ipr014887, Ipr001092 Pfam : PF03931, PF01847 SCOP : d1lqba_, d1lqbb_, d1lqbc_ UniProt : Q15370, Q15369, P40337, Q16665

Functional annotation:
Cellular component:	nucleus cytoplasm membrane cytosol mitochondrion endoplasmic reticulum
Biological process:	protein complex assembly regulation of transcription, DNA-dependent transcription ubiquitin cycle RNA elongation from RNA polymerase II promoter protein modification process regulation of transcription from RNA polymerase II promoter cell cycle anti-apoptosis negative regulation of cell proliferation positive regulation of cell differentiation protein ubiquitination negative regulation of transcription from RNA polymerase II promoter cell morphogenesis response to stress negative regulation of cell cycle proteolysis protein stabilization homeostatic process signal transduction response to hypoxia transcription, DNA-dependent positive regulation of transcription regulation of transcription
Molecular function:	protein binding transcription elongation regulator activity transcription factor binding signal transducer activity transcription regulator activity histone acetyltransferase binding DNA binding RNA polymerase II transcription factor activity, enhancer binding transcription factor activity protein heterodimerization activity

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

Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex

Template:ABSTRACT PUBMED 12050673

About this Structure

1LQB is a 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Hon WC, Wilson MI, Harlos K, Claridge TD, Schofield CJ, Pugh CW, Maxwell PH, Ratcliffe PJ, Stuart DI, Jones EY. Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL. Nature. 2002 Jun 27;417(6892):975-8. Epub 2002 Jun 5. PMID:12050673 doi:https://dx.doi.org/10.1038/nature00767

Page seeded by OCA on Tue Feb 17 21:17:59 2009

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OCA

[1] Hon WC, Wilson MI, Harlos K, Claridge TD, Schofield CJ, Pugh CW, Maxwell PH, Ratcliffe PJ, Stuart DI, Jones EY. Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL. Nature. 2002 Jun 27;417(6892):975-8. Epub 2002 Jun 5. PMID:12050673 doi:https://dx.doi.org/10.1038/nature00767

1lqb | pdb_00001lqb

Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

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