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The Open Protein Structure Annotation Network
PDB Keyword
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Title Crystal structure of Putative amino-acid aminotransferase (YP_265399.1) from Psychrobacter arcticum 273-4 at 2.50 A resolution.
Site JCSG
PDB Id 3if2 Target Id 391142
Molecular Characteristics
Source Psychrobacter arcticum 273-4
Alias Ids YP_265399.1 Molecular Weight 49025.04 Da.
Residues 443 Isoelectric Point 4.93
Sequence mkfskfgqkftqptgisqlmddlgdalksdqpvnmlgggnpakidavnelfletykalgndndtgkanss aiismanysnpqgdsafidalvgffnrhydwnltsenialtngsqnaffylfnlfggafvnehsqdkes ksvdksillpltpeyigysdvhvegqhfaavlphidevthdgeegffkyrvdfealenlpalkegriga iccsrptnptgnvltdeemahlaeiakrydipliidnaygmpfpniiysdahlnwdnntilcfslskig lpgmrtgiivadakvieavsamnavvnlaptrfgaaiatplvandrikqlsdneikpfyqkqatlavkl lkqalgdyplmihkpegaiflwlwfkdlpistldlyerlkakgtlivpseyffpgvdvsdyqhahecir msiaadeqtlidgikvigevvrelydnk
  BLAST   FFAS

Structure Determination
Method XRAY Chains 2
Resolution (Å) 2.50 Rfree 0.221
Matthews' coefficent 2.96 Rfactor 0.178
Waters 203 Solvent Content 58.45

 

Ligand Information
Ligands PLP (PYRIDOXAL-5'-PHOSPHATE) x 2;GOL (GLYCEROL) x 2;ACT (ACETATE) x 1
Metals

Jmol

Protein Summary

The protein YP_265399.1 is annotated as putative valine--pyruvate aminotransferase. YP_265399.1 belongs to PFAM PF00155 Aminotran_1_2 which consists of aminotransferases. These proteins share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. PLP is bound in both the chains in this structure,

 

The monomeric structure is shown below with the ligand PLP bound to it.

MG11417F_mon.png

The protein forms a stable dimer as shown below.

MG11417F.png

 

 

There are several structurally similar proteins as found by a DALI search.

DALI Structural Homologs
N PDB Z-score RMSD LALI NRES %ID TITLE
1 3g7q 52.1 1.5 383 388 46 VALINE-PYRUVATE AMINOTRANSFERASE
2 1gck 39.8 2.5 372 382 22 ASPARTATE AMINOTRANSFERASE
3 1bkg 39.7 2.5 372 382 22 ASPARTATE AMINOTRANSFERASE
4 1gc3 39.6 2.4 372 382 22 ASPARTATE AMINOTRANSFERASE
5 1x0m 39.5 2.4 385 403 22 AMINOTRANSFERASE II HOMOLOGUE
6 1wst 39.5 2.6 387 403 23 MULTIPLE SUBSTRATE AMINOTRANSFERASE
7 1gc4 39.5 2.4 371 382 21 ASPARTATE AMINOTRANSFERASE
8 5bj4 39.4 2.5 359 366 22 PROTEIN (ASPARTATE AMINOTRANSFERASE)
9 1b5p 39.3 2.6 372 382 22 PROTEIN (ASPARTATE AMINOTRANSFERASE)
10 1bjw 39.2 2.6 372 382 21 ASPARTATE AMINOTRANSFERASE

 

Some of these proteins have ligands bound in the same location as this protein. An overall superposition and a zoomed-in view of the active site are shown below.

all.pngall_ligand.png

 

YP_265399.1 (green), 1b5p (cyan), 1bjw (lightmagenta), 1bkg (yellow), 1gc3 (salmon), 1gc4 (lightgrey), 1gck (slate), 1wst (orange), 1x0m (lime), 3g7q (deepteal), 5bj4 (hotpink)
 

 

Literature references
  1. Nakai T, Okada K, Akutsu S, Miyahara I, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K; , Biochemistry 1999;38:2413-2424.: Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate. PUBMED:10029535

  2. Ko TP, Wu SP, Yang WZ, Tsai H, Yuan HS; , Acta Crystallogr D Biol Crystallogr 1999;55:1474-1477.: Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase. PUBMED:10417420

 

Ligand Summary

Reviews

References

 

No references found.

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