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NMR-validated structural model for oxidized R.PALUSTRIS cytochrome C556

Analyse NMR-validated structural model for oxidized R.PALUSTRIS cytochrome C556 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1S05
Type: protein
Length: 129 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C-556
UniProt: P00150
Ligands: HEC
Pockets: 1 · best druggability 0.72

Structure

solution nmr · 1 distinct chain · 61% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C-556	protein	129	61% helix, 0% strand	P00150

Ligands and binding sites

HEC · Heme 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	226	0.72	0.87	34	HEC

Modifications

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

Compared structures

1S05 · NMR-validated structural model for oxidized R.palustris cytochrome c556 · the same entry in another collection · chain A against A, TM-score 1.00
P00150 · AlphaFold monomer V2.0 prediction for cytochrome C-556 (P00150) · a predicted model of the same protein · chain A against A, TM-score 0.85

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 P00150
Elsewhere: RCSB PDB 1S05 · PDBe 1S05 · UniProt P00150

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