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Structure of the human multidrug resistance protein 1 nucleotide binding domain 1

Analyse Structure of the human multidrug resistance protein 1 nucleotide binding domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CBZ
Type: protein
Length: 230 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Multidrug resistance-associated protein 1
UniProt: P33527
Ligands: ATP, MG
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Multidrug resistance-associated protein 1	protein	230	33% helix, 27% strand	P33527

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	54	0.43	0.83	18	empty

Compared structures

2CBZ · Structure of the human Multidrug Resistance Protein 1 Nucleotide Binding Domain 1 · the same entry in another collection · chain A against A, TM-score 1.00
P33527 · AlphaFold monomer V2.0 prediction for multidrug resistance-associated protein 1 (P33527) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P33527
Elsewhere: RCSB PDB 2CBZ · PDBe 2CBZ · UniProt P33527

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