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Structure of P-glycoprotein reveals a molecular basis for poly- specific drug binding

Analyse Structure of P-glycoprotein reveals a molecular basis for poly- specific drug… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3G5U
Type: protein
Length: 2,364 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Multidrug resistance protein 1A
UniProt: Q5I1Y5
Ligands: HG
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 61% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Multidrug resistance protein 1A	protein	1182	61% helix, 8% strand	Q5I1Y5

Ligands and binding sites

HG · Mercury (II) ion · metal · 12 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1027	0.81	0.82	114	empty
2	541	0.77	0.84	91	HG
3	488	0.76	0.84	75	HG
4	766	0.75	0.79	69	empty
5	1034	0.74	0.77	102	empty

Interfaces

1 interface between chains.

A–B · 1351 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

3G5U · Structure of P-glycoprotein Reveals a Molecular Basis for Poly-Specific Drug Binding · 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 Q5I1Y5
Elsewhere: RCSB PDB 3G5U · PDBe 3G5U · UniProt Q5I1Y5

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