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Crystal structure of aqpz mutant T183C complexed with mercury

Analyse Crystal structure of aqpz mutant T183C complexed with mercury in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O9E
Type: protein
Length: 232 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aquaporin Z
UniProt: P60844
Ligands: HG
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aquaporin Z	protein	232	74% helix, 0% strand	P60844

Ligands and binding sites

HG · Mercury (II) ion · metal · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	137	0.53	0.80	32	HG
2	79	0.39	0.77	19	empty

Compared structures

2O9E · Crystal Structure of AqpZ mutant T183C complexed with mercury · the same entry in another collection · chain A against A, TM-score 1.00
P60844 · AlphaFold monomer V2.0 prediction for aquaporin Z (P60844) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P60844
Elsewhere: RCSB PDB 2O9E · PDBe 2O9E · UniProt P60844

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