1b4x: Difference between revisions

Revision as of 14:46, 17 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:1b4x.png

1b4x, resolution 2.45Å (default scene)

Ligands:

MAE, PLP

Activity:

Aspartate transaminase, with EC number 2.6.1.1

Structural annotation:
Resources:	CATH : 1B4Xa01, 1B4Xa02 InterPro : Ipr000796, Ipr004839, Ipr015421, Ipr015424, Ipr004838 Pfam : PF00155 SCOP : d1b4xa_ UniProt : P00509

Functional annotation:
Cellular component:	cytoplasm
Biological process:	biosynthetic process amino acid metabolic process
Molecular function:	pyridoxal phosphate binding catalytic activity transferase activity, transferring nitrogenous groups aspartate transaminase activity transaminase activity protein binding transferase activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

ASPARTATE AMINOTRANSFERASE FROM E. COLI, C191S MUTATION, WITH BOUND MALEATE

Template:ABSTRACT PUBMED 10708649

About this Structure

1B4X is a 1 chain structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Jeffery CJ, Gloss LM, Petsko GA, Ringe D. The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase. Protein Eng. 2000 Feb;13(2):105-12. PMID:10708649

Page seeded by OCA on Tue Feb 17 16:46:50 2009

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Jeffery CJ, Gloss LM, Petsko GA, Ringe D. The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase. Protein Eng. 2000 Feb;13(2):105-12. PMID:10708649

@@ Line 20: / Line 20: @@
 ==About this Structure==
-B4X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4X OCA].
+B4X is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4X OCA].
 ==Reference==
-The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase., Jeffery CJ, Gloss LM, Petsko GA, Ringe D, Protein Eng. 2000 Feb;13(2):105-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10708649 10708649]
+<ref group="xtra">PMID:10708649</ref><references group="xtra"/>
 [[Category: Aspartate transaminase]]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
 [[Category: Gloss, L M.]]
 [[Category: Jeffery, C J.]]
@@ Line 34: / Line 33: @@
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:16:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 16:46:50 2009''

1b4x: Difference between revisions

Revision as of 14:46, 17 February 2009

ASPARTATE AMINOTRANSFERASE FROM E. COLI, C191S MUTATION, WITH BOUND MALEATE

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

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