Mitochondrial amidoxime-reducing component 1

UniProt data

UniProt name: MARC1_HUMAN (Q5VT66)

Gene name: MARC1; Synonyms=MOSC1

Organism: Homo sapiens (Human).

Function: As a component of an N-hydroxylated prodrug-converting complex required to reduce N-hydroxylated prodrugs, such as benzamidoxime. Also able to reduce N(omega)-hydroxy-L-arginine (NOHA) and N(omega)-hydroxy-N(delta)-methyl-L-arginine (NHAM) into L-arginine and N(delta)-methyl-L-arginine, respectively. {ECO:0000269|PubMed:19053771}.

Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:23086957}; Single-pass type II membrane protein {ECO:0000269|PubMed:23086957}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Mitochondrial import is mediated by AA 1-40 and requires ATP.

Transmembrane domains:

  1. 21-40, 20 AA, Helical; Signal-anchor for type II membrane protein. {ECO:0000255}.

Sequence: 337 AA

10 20 30 40 50 60 MGAAGSSALA RFVLLAQSRP GWLGVAALGL TAVALGAVAW RRAWPTRRRR LLQQVGTVAQ 70 80 90 100 110 120 LWIYPVKSCK GVPVSEAECT AMGLRSGNLR DRFWLVINQE GNMVTARQEP RLVLISLTCD 130 140 150 160 170 180 GDTLTLSAAY TKDLLLPIKT PTTNAVHKCR VHGLEIEGRD CGEATAQWIT SFLKSQPYRL 190 200 210 220 230 240 VHFEPHMRPR RPHQIADLFR PKDQIAYSDT SPFLILSEAS LADLNSRLEK KVKATNFRPN 250 260 270 280 290 300 IVISGCDVYA EDSWDELLIG DVELKRVMAC SRCILTTVDP DTGVMSRKEP LETLKSYRQC 310 320 330 DPSERKLYGK SPLFGQYFVL ENPGTIKVGD PVYLLGQ

CATM prediction

The sequence of MARC1_HUMAN returned 1 potential models

The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.

# Sequence and interface d θ Z' ω' Score
    20        30        40  
  |    +    |    +    |   
(Å) (°) (Å) (°)  
SRAGWLGVAALGLTAVALGAVAWRRA 7.2 -46.9° 2.3 44.9 -15.3
SRPGWLGVAALGLTAVALGAVAWRRA          

* Note: this sequence contains Pro residues. CATM substituted them with Ala during the modeling. The positions are marked.

Click on the model number to visualize its details below.

MODEL 1 DETAILS

Precited structure:


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Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 33, VAL, HA A, 32, ALA, O 3.34Å
B, 36, GLY, HA1 A, 33, VAL, O 3.17Å
A, 33, VAL, HA B, 32, ALA, O 3.34Å
A, 36, GLY, HA1 B, 33, VAL, O 3.17Å