6LIG

Crystal structure of human Glutamate oxaloacetate transaminase 1 (GOT1) in complex with AH


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.62 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.217 

Starting Model: experimental
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This is version 1.1 of the entry. See complete history


Literature

Crystal structure of human Glutamate oxaloacetate transaminase 1 (GOT1) in complex with AH

Shan, Y.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Glutamate oxaloacetate transaminase 1
A, B
411Homo sapiensMutation(s): 0 
Gene Names: GOT1
EC: 2.6.1.1 (PDB Primary Data), 2.6.1.3 (PDB Primary Data)
UniProt & NIH Common Fund Data Resources
Find proteins for P17174 (Homo sapiens)
Explore P17174 
Go to UniProtKB:  P17174
PHAROS:  P17174
GTEx:  ENSG00000120053 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP17174
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
EE6 (Subject of Investigation/LOI)
Query on EE6

Download Ideal Coordinates CCD File 
C [auth A]3-[3-(3-methylbut-2-enyl)-4-oxidanyl-phenyl]-5-[[3-(3-methylbut-2-enyl)-4-oxidanyl-phenyl]methylidene]-4-oxidanyl-furan-2-one
C27 H28 O5
LFDYHAWYVIBCDT-UHFFFAOYSA-N
PLP (Subject of Investigation/LOI)
Query on PLP

Download Ideal Coordinates CCD File 
D [auth B]PYRIDOXAL-5'-PHOSPHATE
C8 H10 N O6 P
NGVDGCNFYWLIFO-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.62 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.217 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 64.87α = 90
b = 90.42β = 91.87
c = 74.05γ = 90
Software Package:
Software NamePurpose
Aimlessdata scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
iMOSFLMdata reduction
PHENIXphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2020-12-16
    Type: Initial release
  • Version 1.1: 2023-11-22
    Changes: Data collection, Database references, Refinement description