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Crystal structure of TN501 mera

Analyse Crystal structure of TN501 mera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZX9
Type: protein
Length: 453 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mercuric reductase
EC: 1.16.1.1
UniProt: P00392
Ligands: FAD
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mercuric reductase (EC 1.16.1.1)	protein	453	34% helix, 26% strand	P00392

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	874	0.78	0.81	96	FAD
2	201	0.51	0.77	31	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1ZX9 · Crystal Structure of Tn501 MerA · the same entry in another collection · chain A against A, TM-score 1.00
P00392 · AlphaFold monomer V2.0 prediction for mercuric reductase (P00392) · a predicted model of the same protein · 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 P00392
Elsewhere: RCSB PDB 1ZX9 · PDBe 1ZX9 · UniProt P00392

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