Research workbench

The solution structure of the heme binding variant ARG98CYS of oxidized escherichia COLI cytochrome B562

Analyse The solution structure of the heme binding variant ARG98CYS of oxidized… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QQ3
Type: protein
Length: 106 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome B562
UniProt: P0ABE7
Ligands: HEB
Pockets: 1 · best druggability 0.59

Structure

solution nmr · 1 distinct chain · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome B562	protein	106	75% helix, 0% strand	P0ABE7

Ligands and binding sites

HEB · Heme B/C · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	124	0.59	0.84	24	HEB

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

1QQ3 · The solution structure of the heme binding variant ARG98CYS of oxidized escherichia COLI… · the same entry in another collection · chain A against A, TM-score 1.00
P0ABE7 · AlphaFold monomer V2.0 prediction for soluble cytochrome B562 (P0ABE7) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 P0ABE7
Elsewhere: RCSB PDB 1QQ3 · PDBe 1QQ3 · UniProt P0ABE7

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.