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- EMDB-64896: Structure of the ACE2-B0AT1 bound with tryptophan -

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Basic information

Entry
Database: EMDB / ID: EMD-64896
TitleStructure of the ACE2-B0AT1 bound with tryptophan
Map data
Sample
  • Complex: Structure of the ACE2-B0AT1 bound with tryptophan
    • Protein or peptide: Angiotensin-converting enzyme 2
    • Protein or peptide: Sodium-dependent neutral amino acid transporter B(0)AT1
  • Ligand: TRYPTOPHAN
Keywordscomplex / membrane protein / amino acid
Function / homology
Function and homology information


Defective transport of neurotransmitters by SLC6A19 causes Hartnup disorder (HND) / Defective transport of amino acids by SLC6A19 causes Hartnup disorder (HND) / neutral amino acid transport / neutral L-amino acid transmembrane transporter activity / Amino acid transport across the plasma membrane / symporter activity / amino acid transmembrane transporter activity / SLC-mediated transport of neurotransmitters / positive regulation of amino acid transport / angiotensin-converting enzyme 2 ...Defective transport of neurotransmitters by SLC6A19 causes Hartnup disorder (HND) / Defective transport of amino acids by SLC6A19 causes Hartnup disorder (HND) / neutral amino acid transport / neutral L-amino acid transmembrane transporter activity / Amino acid transport across the plasma membrane / symporter activity / amino acid transmembrane transporter activity / SLC-mediated transport of neurotransmitters / positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / angiotensin-mediated drinking behavior / amino acid transport / positive regulation of gap junction assembly / tryptophan transport / regulation of systemic arterial blood pressure by renin-angiotensin / maternal process involved in female pregnancy / regulation of cardiac conduction / peptidyl-dipeptidase activity / transporter activator activity / regulation of vasoconstriction / Metabolism of Angiotensinogen to Angiotensins / carboxypeptidase activity / angiotensin maturation / viral life cycle / receptor-mediated endocytosis of virus by host cell / Attachment and Entry / metallocarboxypeptidase activity / positive regulation of cardiac muscle contraction / response to nutrient / regulation of cytokine production / blood vessel diameter maintenance / sodium ion transmembrane transport / negative regulation of smooth muscle cell proliferation / brush border membrane / negative regulation of ERK1 and ERK2 cascade / positive regulation of reactive oxygen species metabolic process / metallopeptidase activity / endocytic vesicle membrane / regulation of cell population proliferation / virus receptor activity / regulation of inflammatory response / endopeptidase activity / Induction of Cell-Cell Fusion / Potential therapeutics for SARS / membrane fusion / Attachment and Entry / entry receptor-mediated virion attachment to host cell / receptor-mediated virion attachment to host cell / apical plasma membrane / cilium / membrane raft / endoplasmic reticulum lumen / symbiont entry into host cell / cell surface / negative regulation of transcription by RNA polymerase II / : / extracellular exosome / extracellular region / zinc ion binding / membrane / identical protein binding / plasma membrane
Similarity search - Function
Neutral amino acid SLC6 transporter / Sodium:neurotransmitter symporter family signature 1. / Sodium:neurotransmitter symporter / Sodium:neurotransmitter symporter superfamily / Sodium:neurotransmitter symporter family / Sodium:neurotransmitter symporter family profile. / Collectrin domain / Renal amino acid transporter / Collectrin-like domain profile. / Peptidase M2, peptidyl-dipeptidase A ...Neutral amino acid SLC6 transporter / Sodium:neurotransmitter symporter family signature 1. / Sodium:neurotransmitter symporter / Sodium:neurotransmitter symporter superfamily / Sodium:neurotransmitter symporter family / Sodium:neurotransmitter symporter family profile. / Collectrin domain / Renal amino acid transporter / Collectrin-like domain profile. / Peptidase M2, peptidyl-dipeptidase A / Angiotensin-converting enzyme / Peptidase family M2 domain profile. / Neutral zinc metallopeptidases, zinc-binding region signature.
Similarity search - Domain/homology
Sodium-dependent neutral amino acid transporter B(0)AT1 / Angiotensin-converting enzyme 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.24 Å
AuthorsYan RH / Zhang T
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Oral Science and Homeostatic Medicine / Year: 2025
Title: Structural basis of aromatic amino acid recognition by the human ACE2-B0AT1 transporter complex
Authors: Zhang T / Zeng Q / Xu C / Liang H / Zhang S / Wang Z / Yan R
History
DepositionJun 2, 2025-
Header (metadata) releaseMay 13, 2026-
Map releaseMay 13, 2026-
UpdateMay 13, 2026-
Current statusMay 13, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_64896.png

Downloads & links

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Map

FileDownload / File: emd_64896.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.86 Å/pix.
x 360 pix.
= 307.8 Å		0.86 Å/pix.
x 360 pix.
= 307.8 Å		0.86 Å/pix.
x 360 pix.
= 307.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.855 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.22
Minimum - Maximum-1.6878705 - 2.5147955
Average (Standard dev.)0.0006157169 (±0.054804187)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 307.80002 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_64896_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_64896_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : Structure of the ACE2-B0AT1 bound with tryptophan

EntireName: Structure of the ACE2-B0AT1 bound with tryptophan
Components
  • Complex: Structure of the ACE2-B0AT1 bound with tryptophan
    • Protein or peptide: Angiotensin-converting enzyme 2
    • Protein or peptide: Sodium-dependent neutral amino acid transporter B(0)AT1
  • Ligand: TRYPTOPHAN

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Supramolecule #1: Structure of the ACE2-B0AT1 bound with tryptophan

SupramoleculeName: Structure of the ACE2-B0AT1 bound with tryptophan / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Angiotensin-converting enzyme 2

MacromoleculeName: Angiotensin-converting enzyme 2 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: angiotensin-converting enzyme 2
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 93.504578 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: WSHPQFEKQS TIEEQAKTFL DKFNHEAEDL FYQSSLASWN YNTNITEENV QNMNNAGDKW SAFLKEQSTL AQMYPLQEIQ NLTVKLQLQ ALQQNGSSVL SEDKSKRLNT ILNTMSTIYS TGKVCNPDNP QECLLLEPGL NEIMANSLDY NERLWAWESW R SEVGKQLR ...String:
WSHPQFEKQS TIEEQAKTFL DKFNHEAEDL FYQSSLASWN YNTNITEENV QNMNNAGDKW SAFLKEQSTL AQMYPLQEIQ NLTVKLQLQ ALQQNGSSVL SEDKSKRLNT ILNTMSTIYS TGKVCNPDNP QECLLLEPGL NEIMANSLDY NERLWAWESW R SEVGKQLR PLYEEYVVLK NEMARANHYE DYGDYWRGDY EVNGVDGYDY SRGQLIEDVE HTFEEIKPLY EHLHAYVRAK LM NAYPSYI SPIGCLPAHL LGDMWGRFWT NLYSLTVPFG QKPNIDVTDA MVDQAWDAQR IFKEAEKFFV SVGLPNMTQG FWE NSMLTD PGNVQKAVCH PTAWDLGKGD FRILMCTKVT MDDFLTAHHE MGHIQYDMAY AAQPFLLRNG ANEGFHEAVG EIMS LSAAT PKHLKSIGLL SPDFQEDNET EINFLLKQAL TIVGTLPFTY MLEKWRWMVF KGEIPKDQWM KKWWEMKREI VGVVE PVPH DETYCDPASL FHVSNDYSFI RYYTRTLYQF QFQEALCQAA KHEGPLHKCD ISNSTEAGQK LFNMLRLGKS EPWTLA LEN VVGAKNMNVR PLLNYFEPLF TWLKDQNKNS FVGWSTDWSP YADQSIKVRI SLKSALGDKA YEWNDNEMYL FRSSVAY AM RQYFLKVKNQ MILFGEEDVR VANLKPRISF NFFVTAPKNV SDIIPRTEVE KAIRMSRSRI NDAFRLNDNS LEFLGIQP T LGPPNQPPVS IWLIVFGVVM GVIVVGIVIL IFTGIRDRKK KNKARSGENP YASIDISKGE NNPGFQNTDD VQTSFLEHH HHHHHHHH

UniProtKB: Angiotensin-converting enzyme 2

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Macromolecule #2: Sodium-dependent neutral amino acid transporter B(0)AT1

MacromoleculeName: Sodium-dependent neutral amino acid transporter B(0)AT1
type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 73.087086 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: DYKDDDDKSG PDEVDASGRV RLVLPNPGLD ARIPSLAELE TIEQEEASSR PKWDNKAQYM LTCLGFCVGL GNVWRFPYLC QSHGGGAFM IPFLILLVLE GIPLLYLEFA IGQRLRRGSL GVWSSIHPAL KGLGLASMLT SFMVGLYYNT IISWIMWYLF N SFQEPLPW ...String:
DYKDDDDKSG PDEVDASGRV RLVLPNPGLD ARIPSLAELE TIEQEEASSR PKWDNKAQYM LTCLGFCVGL GNVWRFPYLC QSHGGGAFM IPFLILLVLE GIPLLYLEFA IGQRLRRGSL GVWSSIHPAL KGLGLASMLT SFMVGLYYNT IISWIMWYLF N SFQEPLPW SDCPLNENQT GYVDECARSS PVDYFWYRET LNISTSISDS GSIQWWMLLC LACAWSVLYM CTIRGIETTG KA VYITSTL PYVVLTIFLI RGLTLKGATN GIVFLFTPNV TELAQPDTWL DAGAQVFFSF SLAFGGLISF SSYNSVHNNC EKD SVIVSI INGFTSVYVA IVVYSVIGFR ATQRYDDCFS TNILTLINGF DLPEGNVTQE NFVDMQQRCN ASDPAAYAQL VFQT CDINA FLSEAVEGTG LAFIVFTEAI TKMPLSPLWS VLFFIMLFCL GLSSMFGNME GVVVPLQDLR VIPPKWPKEV LTGLI CLGT FLIGFIFTLN SGQYWLSLLD SYAGSIPLLI IAFCEMFSVV YVYGVDRFNK DIEFMIGHKP NIFWQVTWRV VSPLLM LII FLFFFVVEVS QELTYSIWDP GYEEFPKSQK ISYPNWVYVV VVIVAGVPSL TIPGYAIYKL IRNHCQKPGD HQGLVST LS TASMNGDLKY

UniProtKB: Sodium-dependent neutral amino acid transporter B(0)AT1

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Macromolecule #3: TRYPTOPHAN

MacromoleculeName: TRYPTOPHAN / type: ligand / ID: 3 / Number of copies: 2 / Formula: TRP
Molecular weightTheoretical: 204.225 Da
Chemical component information

ChemComp-TRP:
TRYPTOPHAN

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 5.0 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

8i92

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.24 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 140545
Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER

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