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Outer membrane protein cusc

Analyse Outer membrane protein cusc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PIK
Type: protein
Length: 429 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cation efflux system protein cusc
UniProt: P77211
Ligands: UNL, SO4
Pockets: 5 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 64% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cation efflux system protein cusc	protein	429	64% helix, 12% strand	P77211

Ligands and binding sites

UNL · Unknown ligand · ligand · 2 copies · chains A
SO4 · Sulfate ion · ion · 7 copies · chains A

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	96	0.43	0.78	21	empty
2	70	0.40	0.80	17	empty
3	61	0.34	0.77	14	empty
4	68	0.32	0.75	16	SO4
5	78	0.29	0.72	25	empty

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

3PIK · Outer membrane protein CusC · the same entry in another collection · chain A against A, TM-score 1.00
P77211 · AlphaFold monomer V2.0 prediction for cation efflux system protein cusc (P77211) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P77211
Elsewhere: RCSB PDB 3PIK · PDBe 3PIK · UniProt P77211

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