9KXV | pdb_00009kxv

Structure of human B0AT1-ACE2 complex with compound3

Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.71 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history. 


Literature

Structure-guided development of a potent human B0AT1 inhibitor effective in a mouse model of phenylketonuria

Imazu, T., Akashi, T., Hiraizumi, M., Inui, Y., Sasaki, W., Takahashi, T., Todoroki, H., Kumanomidou, T., Hisano, H., Asada, H., Kusakizako, T., Nishizawa, T., Iwata, S., Nureki, O., Miyaguchi, I.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Sodium-dependent neutral amino acid transporter B(0)AT1654Homo sapiensMutation(s): 0 
Gene Names: SLC6A19, B0AT1
UniProt & NIH Common Fund Data Resources
Find proteins for Q695T7 (Homo sapiens)
Explore Q695T7 
Go to UniProtKB:  Q695T7
PHAROS:  Q695T7
GTEx:  ENSG00000174358 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ695T7
Glycosylation
Glycosylation Sites: 1
Go to GlyGen: Q695T7-1
Sequence Annotations
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  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Angiotensin-converting enzyme 2806Homo sapiensMutation(s): 0 
Gene Names: ACE2, UNQ868/PRO1885
EC: 3.4.17.23 (PDB Primary Data), 3.4.17 (PDB Primary Data)
UniProt & NIH Common Fund Data Resources
Find proteins for Q9BYF1 (Homo sapiens)
Explore Q9BYF1 
Go to UniProtKB:  Q9BYF1
PHAROS:  Q9BYF1
GTEx:  ENSG00000130234 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9BYF1
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
A1L6W (Subject of Investigation/LOI)
Query on A1L6W
Download Ideal Coordinates CCD File 
D [auth A](~{E})-~{N}-[2-oxidanylidene-2-(3-oxidanylidenepiperazin-1-yl)ethyl]-3-[4-(trifluoromethyl)phenyl]prop-2-enamide
C16 H16 F3 N3 O3
SQCPJGHMDVTIRR-ZZXKWVIFSA-N
NAG
Query on NAG
Download Ideal Coordinates CCD File 
C [auth A]2-acetamido-2-deoxy-beta-D-glucopyranose
C8 H15 N O6
OVRNDRQMDRJTHS-FMDGEEDCSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.71 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
MODEL REFINEMENTREFMAC5.8.0267

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
Not funded--

Revision History  (Full details and data files)

  • Version 1.0: 2025-12-10
    Type: Initial release