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Structure of the periplasmic adaptor protein emra

Analyse Structure of the periplasmic adaptor protein emra in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TKO
Type: protein
Length: 326 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Emra
UniProt: O67159
Ligands: MG

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Emra	protein	326	45% helix, 25% strand	O67159

Ligands and binding sites

MG · Magnesium ion · metal · chains B
IPA · Isopropyl alcohol · additive · 2 copies · chains B

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

Compared structures

4TKO · Structure of the periplasmic adaptor protein EmrA · the same entry in another collection · chain B against B, TM-score 1.00

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 O67159
Elsewhere: RCSB PDB 4TKO · PDBe 4TKO · UniProt O67159

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