Research workbench

X-ray structure of the M100K variant of ferric cyt C-550 from paracoccus versutus determined at 295 K.

Analyse X-ray structure of the M100K variant of ferric cyt C-550 from paracoccus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BH5
Type: protein
Length: 121 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C-550
UniProt: Q00499
Ligands: HEC
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Cytochrome C-550	protein	121	39% helix, 6% strand	Q00499

Ligands and binding sites

HEC · Heme C · ligand · chains X

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	239	0.77	0.90	35	HEC

Modifications

Observed in the structure: 2 cofactor (heme c attachment).

Compared structures

2BH5 · X-ray structure of the M100K variant of ferric cyt c-550 from Paracoccus versutus… · the same entry in another collection · chain X against X, TM-score 1.00
Q00499 · AlphaFold monomer V2.0 prediction for cytochrome C-550 (Q00499) · a predicted model of the same protein · chain X 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 Q00499
Elsewhere: RCSB PDB 2BH5 · PDBe 2BH5 · UniProt Q00499

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