Research workbench

Structure of emre-D3 mutant in complex with monobody L10 and harmane

Analyse Structure of emre-D3 mutant in complex with monobody L10 and harmane in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7SVX
Type: protein
Length: 382 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P23895
Ligands: CN9

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	103	—	P23895
C	—	protein	90	—	—
B	—	protein	100	—	P23895
D	—	protein	89	—	—

Ligands and binding sites

CN9 · 1-methyl-9H-pyrido[3,4-b]indole · ligand · chains A, B

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

Compared structures

7SVX · Structure of EmrE-D3 mutant in complex with monobody L10 and harmane · the same entry in another collection · chain A against A, TM-score 1.00
P23895 · AlphaFold monomer V2.0 prediction for multidrug transporter emre (P23895) · a predicted model of the same protein · chain A against A, TM-score 0.83
2I68 · Cryo-EM based theoretical model structure of transmembrane domain of the… · a predicted model of the same protein · chain A against A, TM-score 0.63
2I68 · Cryo-EM based theoretical model structure of transmembrane domain of the… · a predicted model of the same protein · chain A against A, TM-score 0.63

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 P23895
Elsewhere: RCSB PDB 7SVX · PDBe 7SVX · UniProt P23895

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