Research workbench

MamM CTD - Copper form

Analyse MamM CTD - Copper form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GP6
Type: protein
Length: 194 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.146
Source: Magnetospirillum gryphiswaldense MSR-1
Molecule: Magnetosome protein MamM
UniProt: Q6NE57
Ligands: CU
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · resolution 2.146 · 2 distinct chains · 35% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Magnetosome protein MamM	protein	103	36% helix, 32% strand	Q6NE57
B	Magnetosome protein MamM	protein	91	34% helix, 33% strand	Q6NE57

Ligands and binding sites

CU · Copper (II) ion · metal · 3 copies · chains A, B
BME · Beta-mercaptoethanol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	540	0.69	0.78	48	CU, BME

Interfaces

1 interface between chains.

A–B · 771 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

6GP6 · Mamm ctd - copper form · the same entry in another collection · chain A against A, 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 Q6NE57
Elsewhere: RCSB PDB 6GP6 · PDBe 6GP6 · UniProt Q6NE57

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