MolNFT v1 · #149285 · protein

Crystal structure of human MARC1

6FW2: “Crystal structure of human MARC1”. X-ray diffraction, 4 ligands (MTE, EFK, MOO). MolNFT v1 #149285 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6FW2
Type: protein
Length: 444 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q5VT66, D9IEF7
Ligands: MTE, EFK, MOO, PO4

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	444	—	Q5VT66, D9IEF7

Ligands and binding sites

MTE · Phosphonic acidmono-(2-amino-5,6-dimercapto-4-oxo-3,7,8A,9,10,10A-hexahydro-4H-8-oxa-1,3,9,10-tetraaza-anthracen-7-ylmethyl)ester · ligand · chains A
EFK · oxidanyl(oxidanylidene)molybdenum · ligand · chains A
MOO · Molybdate ion · ion · 4 copies · chains A
PO4 · Phosphate ion · ion · chains A
B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6FW2 · Crystal Structure of human mARC1 · the same entry in another collection · chain A against A, TM-score 1.00
Q5VT66 · AlphaFold monomer V2.0 prediction for mitochondrial amidoxime- reducing component 1… · a predicted model of the same protein · chain A against A, TM-score 0.64

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q5VT66
Every structure of UniProt D9IEF7
Elsewhere: RCSB PDB 6FW2 · PDBe 6FW2 · UniProt Q5VT66 · UniProt D9IEF7

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