MolNFT v1 · #181710 · protein

The structure of bacillus subtilis bmrcd in the inward-facing conformation bound to hoechst-33342 and ATP

7M33: “The structure of bacillus subtilis bmrcd in the inward-facing conformation bound to hoechst-33342 and ATP”. Electron microscopy, 2 ligands (ATP, HT1). MolNFT v1 #181710 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7M33
Type: protein
Length: 1,237 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: O07550, O07549
Ligands: ATP, HT1

Structure

electron microscopy · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	—	protein	573	—	O07550
D	—	protein	664	—	O07549

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains C, D
HT1 · 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bi-benzimidazole · ligand · 2 copies · chains C, D

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

Compared structures

7M33 · The structure of Bacillus subtilis BmrCD in the inward-facing conformation bound to… · the same entry in another collection · chain C against C, TM-score 1.00
O07550 · AlphaFold monomer V2.0 prediction for probable multidrug resistance ABC transporter… · a predicted model of the same protein · chain C against A, TM-score 0.93
O07549 · AlphaFold monomer V2.0 prediction for probable multidrug resistance ABC transporter… · a predicted model of the same protein · chain D against A, TM-score 0.93

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 O07550
Every structure of UniProt O07549
Elsewhere: RCSB PDB 7M33 · PDBe 7M33 · UniProt O07550 · UniProt O07549

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